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Keywords = disulphide bridging

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10 pages, 1300 KiB  
Perspective
The Molecular Pathology of Pre-Eclamptic Hypertension
by Robin W. Carrell, Randy J. Read and Aiwu Zhou
Curr. Issues Mol. Biol. 2025, 47(5), 375; https://doi.org/10.3390/cimb47050375 - 20 May 2025
Viewed by 400
Abstract
The central role of angiotensinogen in the control of blood pressure is revealed by a series of crystallographic structures, including complexes with renin. Specifically, the structures provide an understanding of the sequential molecular events that lead to the pre-eclamptic hypertensive crises of pregnancy. [...] Read more.
The central role of angiotensinogen in the control of blood pressure is revealed by a series of crystallographic structures, including complexes with renin. Specifically, the structures provide an understanding of the sequential molecular events that lead to the pre-eclamptic hypertensive crises of pregnancy. The release of the precursor vasopressor peptide from the amino-terminal tail of angiotensinogen appears to be modulated by a redox-sensitive disulphide bridge. Our findings indicate that the activation of the thiol-switch in the circulating maternal angiotensinogen occurs at the placental level in response to oxidative stress, exacerbated by placental insufficiency. We propose here that a contributory factor is the inherent redox stress accompanying the placental exchange of oxygenation between the haemoglobin of the mother (oxy-HbA) and the deoxygenated haemoglobin of the foetus (deoxy-HbF). Full article
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13 pages, 1495 KiB  
Article
A Simple Analysis of the Second (Extra) Disulfide Bridge of VHHs
by Carla Martins, Fabrice Gardebien, Aravindan Arun Nadaradjane, Julien Diharce and Alexandre G. de Brevern
Molecules 2024, 29(20), 4863; https://doi.org/10.3390/molecules29204863 - 14 Oct 2024
Viewed by 1241
Abstract
Camelids produce a special type of antibody, known as VHHs, that has lost the VL domain, providing a more optimised VH domain. This particular highly stable antibody domain has interesting properties for biotechnological development. Ordinarily, those molecules possess only [...] Read more.
Camelids produce a special type of antibody, known as VHHs, that has lost the VL domain, providing a more optimised VH domain. This particular highly stable antibody domain has interesting properties for biotechnological development. Ordinarily, those molecules possess only one disulphide bridge, but surprisingly, at least a quarter of these VHHs have a second one. Curiously, this does not seem to be essential for the stability and the function of this domain. In an attempt to characterise precisely the role and impact of this disulphide bridge at the molecular level, several in silico mutants of a VHH were created to disrupt this second disulphide bridge and those systems were submitted to molecular dynamics simulation. The loss of the second disulphide bridge leads to an increase in the flexibility of CDR1 and CDR3 and an unexpected rigidification of CDR2. Local conformational analysis shows local differences in the observed protein conformations. However, in fact, there is no exploration of new conformations but a change in the equilibrium between the different observed conformations. This explains why the interaction of VHHs is not really affected by the presence or absence of this second bridge, but their rigidity is slightly reduced. Therefore, the additional disulphide bridge does not seem to be an essential part of VHHs function. Full article
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22 pages, 6146 KiB  
Article
The Antimicrobial Peptide Capitellacin: Chemical Synthesis of Analogues to Probe the Role of Disulphide Bridges and Their Replacement with Vinyl Sulphides
by Oscar A. Shepperson, Paul W. R. Harris, Margaret A. Brimble and Alan J. Cameron
Antibiotics 2024, 13(7), 615; https://doi.org/10.3390/antibiotics13070615 - 2 Jul 2024
Cited by 2 | Viewed by 1947
Abstract
Capitellacin (1) is a 20-residue antimicrobial β-hairpin, produced by the marine polychaeta (segmented worms) Capitella teletai. Since its discovery in 2020, only very limited studies have been undertaken to understand capitellacin’s structure–activity relationship (SAR). Using fast-flow Fmoc-SPPS, a focused library [...] Read more.
Capitellacin (1) is a 20-residue antimicrobial β-hairpin, produced by the marine polychaeta (segmented worms) Capitella teletai. Since its discovery in 2020, only very limited studies have been undertaken to understand capitellacin’s structure–activity relationship (SAR). Using fast-flow Fmoc-SPPS, a focused library of capitellacin analogues was prepared to systematically study the influence of the two disulphide bridges on its structure and activity, and their replacement with a vinyl sulphide as a potential bioisostere. Upon studying the resulting peptides’ antimicrobial activity and secondary structure, the most terminal disulphide emerged as the most critical element for maintaining both bioactivity and the secondary structure, properties which were demonstrated to be closely interlinked. The removal of the innermost disulphide bridge or disulphide replacement with a vinyl sulphide emerged as strategies with which to tune the activity spectrum, producing selectivity towards E. coli. Additionally, an enantiomeric d-capitellacin analogue revealed mechanistic insights, suggesting that chirality may be an inherent property of capitellacin’s bacterial membrane target, or that a hitherto unknown secondary mechanism of action may exist. Additionally, we propose the Alloc protecting group as a more appropriate alternative to the common Dde group during fast-flow Fmoc-SPPS, in particular for short-chain diamino acids. Full article
(This article belongs to the Special Issue Recent Advances in Antimicrobial Drug Discovery, 2nd Edition)
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26 pages, 2059 KiB  
Review
The MUC2 Gene Product: Polymerisation and Post-Secretory Organisation—Current Models
by Kyle J. Stanforth, Maria I. Zakhour, Peter I. Chater, Matthew D. Wilcox, Beth Adamson, Niamh A. Robson and Jeffrey P. Pearson
Polymers 2024, 16(12), 1663; https://doi.org/10.3390/polym16121663 - 12 Jun 2024
Cited by 4 | Viewed by 2862
Abstract
MUC2 mucin, the primary gel-forming component of intestinal mucus, is well researched and a model of polymerisation and post-secretory organisation has been published previously. Recently, several significant developments have been made which either introduce new ideas or challenge previous theories. New ideas include [...] Read more.
MUC2 mucin, the primary gel-forming component of intestinal mucus, is well researched and a model of polymerisation and post-secretory organisation has been published previously. Recently, several significant developments have been made which either introduce new ideas or challenge previous theories. New ideas include an overhaul of the MUC2 C-terminal globular structure which is proposed to harbour several previously unobserved domains, and include a site for an extra intermolecular disulphide bridge dimer between the cysteine 4379 of adjacent MUC2 C-termini. MUC2 polymers are also now thought to be secreted attached to the epithelial surface of goblet cells in the small intestine and removed following secretion via a metalloprotease meprin β-mediated cleavage of the von Willebrand D2 domain of the N-terminus. It remains unclear whether MUC2 forms intermolecular dimers, trimers, or both, at the N-termini during polymerisation, with several articles supporting either trimer or dimer formation. The presence of a firm inner mucus layer in the small intestine is similarly unclear. Considering this recent research, this review proposes an update to the previous model of MUC2 polymerisation and secretion, considers conflicting theories and data, and highlights the importance of this research to the understanding of MUC2 mucus layers in health and disease. Full article
(This article belongs to the Section Biobased and Biodegradable Polymers)
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27 pages, 5346 KiB  
Article
Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro
by Natalie Young, Zizhao Gui, Suleiman Mustafa, Kleopatra Papa, Emily Jessop, Elizabeth Ruddell, Laura Bevington, Roy A. Quinlan, Adam M. Benham, Martin W. Goldberg, Boguslaw Obara and Iakowos Karakesisoglou
Cells 2024, 13(11), 906; https://doi.org/10.3390/cells13110906 - 24 May 2024
Viewed by 2752
Abstract
Eukaryotic cells tether the nucleoskeleton to the cytoskeleton via a conserved molecular bridge, called the LINC complex. The core of the LINC complex comprises SUN-domain and KASH-domain proteins that directly associate within the nuclear envelope lumen. Intra- and inter-chain disulphide bonds, along with [...] Read more.
Eukaryotic cells tether the nucleoskeleton to the cytoskeleton via a conserved molecular bridge, called the LINC complex. The core of the LINC complex comprises SUN-domain and KASH-domain proteins that directly associate within the nuclear envelope lumen. Intra- and inter-chain disulphide bonds, along with KASH-domain protein interactions, both contribute to the tertiary and quaternary structure of vertebrate SUN-domain proteins. The significance of these bonds and the role of PDIs (protein disulphide isomerases) in LINC complex biology remains unclear. Reducing and non-reducing SDS-PAGE analyses revealed a prevalence of SUN2 homodimers in non-tumorigenic breast epithelia MCF10A cells, but not in the invasive triple-negative breast cancer MDA-MB-231 cell line. Furthermore, super-resolution microscopy revealed SUN2 staining alterations in MCF10A, but not in MDA-MB-231 nuclei, upon reducing agent exposure. While PDIA1 levels were similar in both cell lines, pharmacological inhibition of PDI activity in MDA-MB-231 cells led to SUN-domain protein down-regulation, as well as Nesprin-2 displacement from the nucleus. This inhibition also caused changes in perinuclear cytoskeletal architecture and lamin downregulation, and increased the invasiveness of PDI-inhibited MDA-MB-231 cells in space-restrictive in vitro environments, compared to untreated cells. These results emphasise the key roles of PDIs in regulating LINC complex biology, cellular architecture, biomechanics, and invasion. Full article
(This article belongs to the Special Issue Cytoskeletal Remodeling in Health and Disease)
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22 pages, 7197 KiB  
Article
Progressive Design of a Ranatuerin-2 Peptide from Amolops wuyiensis: Enhancement of Bioactivity and In Vivo Efficacy
by Aifang Yao, Tianxing Liu, Yuhai Cai, Siqi Zhou, Xiaoling Chen, Mei Zhou, Chengbang Ma, Tianbao Chen, Chris Shaw and Lei Wang
Antibiotics 2024, 13(1), 5; https://doi.org/10.3390/antibiotics13010005 - 19 Dec 2023
Cited by 6 | Viewed by 2349
Abstract
Antimicrobial peptides (AMPs) that exert multiple functions are considered promising candidates to combat the bacterial drug resistance crisis. Nowadays, targeted peptide modification has been widely recognised to improve biological activity and make up for deficiencies in clinical applications such as toxicity. In this [...] Read more.
Antimicrobial peptides (AMPs) that exert multiple functions are considered promising candidates to combat the bacterial drug resistance crisis. Nowadays, targeted peptide modification has been widely recognised to improve biological activity and make up for deficiencies in clinical applications such as toxicity. In this study, a helix-loop peptide was isolated and identified from the skin secretion of the Wuyi torrent frog Amolops wuyiensis, namely, ranatuerin-2-AW (R2AW) (GFMDTAKNVAKNVAATLLDKLKCKITGGC). Target modifications were made to R2AW to study the structure–activity relationships and to optimise its bioactivities. Five analogues were progressively designed via residue substitution and truncation and the antibacterial and anticancer activities were evaluated. We found that the serine-substitution and cyclic-domain-deletion products showed similar antibacterial activity to the natural peptide R2AW, implying that the disulphide bridge and Rana box were dispensable for the antibacterial activity of ranatuerin-2 peptides. Notably, the cationicity- and hydrophobicity-enhanced variant, [Lys4,19, Leu20]R2AW(1-22)-NH2, exhibited significantly optimised antibacterial and anticancer activities. Additionally, it killed bacteria by membrane disruption at a highly efficient rate. Moreover, [Lys4,19, Leu20]R2AW(1-22)-NH2 exerted potential in vivo efficacy in a methicillin-resistant Staphylococcus aureus (MRSA)-infected waxworm model. Overall, this study demonstrated some rational design ideas for optimising the dual antibacterial and anticancer activities of ranatuerin-2 peptides and it proposes [Lys4,19, Leu20]R2AW(1-22)-NH2 as an appealing candidate for therapeutic development. Full article
(This article belongs to the Special Issue Design, Modification and Application of Antimicrobial Peptides)
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25 pages, 5519 KiB  
Article
Defensin Interactions in Relation to Monoclonal and Disease-Related Proteinase 3 Antibodies Binding at the Catalytic Site
by Morten Zoega, Nicole Hartwig Trier, Rikke Guldhammer Nejrup, Anna Chailyan, Tina Friis, Peter Højrup and Gunnar Houen
Antibodies 2023, 12(1), 23; https://doi.org/10.3390/antib12010023 - 13 Mar 2023
Viewed by 2871
Abstract
Proteinase 3 (PR3) is a neutrophil granulocyte enzyme and an autoantigen found in several forms of vasculitis. Due to the diagnostic and clinical importance of antibodies (Abs) to PR3, it is important to characterize the protein and the nature of its epitopes. Here, [...] Read more.
Proteinase 3 (PR3) is a neutrophil granulocyte enzyme and an autoantigen found in several forms of vasculitis. Due to the diagnostic and clinical importance of antibodies (Abs) to PR3, it is important to characterize the protein and the nature of its epitopes. Here, we have characterized PR3 monoclonal antibodies (MAbs) and disease-associated Abs and their dependency on the PR3 structure and modifications, especially interactions with α-defensins. Three MAbs (HYB 172-01, 172-04, 172-05), which bind to PR3 in its native and denatured forms and provide the disulphide bridges, were intact. α-1-antitrypsin (AT) binds to purified human neutrophil granulocyte PR3 and inhibits its proteolytic activity, towards a small synthetic peptide substrate and a large protein substrate (casein). AT also inhibited the binding of the three MAbs to PR3, indicating that they bind in a region affected by AT binding. However, the MAbs did not inhibit PR3 proteolytic activity with a small substrate, showing that they bound at the active site without restricting access to the substrate cleft. Patient-derived Abs showed essentially the same characteristics as the MAbs, with important implications for vasculitis diagnostics and pathophysiology. Current findings illustrate that PR3 epitopes depend on the three-dimensional structure of the PR3/defensin complex, and that the epitopes depend to a smaller or larger degree on PR3/defensin associations. Full article
(This article belongs to the Special Issue Antibodies: 10th Anniversary)
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13 pages, 1184 KiB  
Review
Secretory Phospholipases A2, from Snakebite Envenoming to a Myriad of Inflammation Associated Human Diseases—What Is the Secret of Their Activity?
by Fiorella Tonello
Int. J. Mol. Sci. 2023, 24(2), 1579; https://doi.org/10.3390/ijms24021579 - 13 Jan 2023
Cited by 3 | Viewed by 3034
Abstract
Secreted phospholipases of type A2 (sPLA2s) are proteins of 14–16 kDa present in mammals in different forms and at different body sites. They are involved in lipid transformation processes, and consequently in various immune, inflammatory, and metabolic processes. sPLA2s are also major components [...] Read more.
Secreted phospholipases of type A2 (sPLA2s) are proteins of 14–16 kDa present in mammals in different forms and at different body sites. They are involved in lipid transformation processes, and consequently in various immune, inflammatory, and metabolic processes. sPLA2s are also major components of snake venoms, endowed with various toxic and pharmacological properties. The activity of sPLA2s is not limited to the enzymatic one but, through interaction with different types of molecules, they exert other activities that are still little known and explored, both outside and inside the cells, as they can be endocytosed. The aim of this review is to analyze three features of sPLA2s, yet under-explored, knowledge of which could be crucial to understanding the activity of these proteins. The first feature is their disulphide bridge pattern, which has always been considered immutable and necessary for their stability, but which might instead be modulable. The second characteristic is their ability to undergo various post-translational modifications that would control their interaction with other molecules. The third feature is their ability to participate in active molecular condensates both on the surface and within the cell. Finally, the implications of these features in the design of anti-inflammatory drugs are discussed. Full article
(This article belongs to the Special Issue Lipid Signaling and Metabolism in Inflammation-Associated Diseases)
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18 pages, 3709 KiB  
Article
Functional Analysis of Conserved Hypothetical Proteins from the Antarctic Bacterium, Pedobacter cryoconitis Strain BG5 Reveals Protein Cold Adaptation and Thermal Tolerance Strategies
by Makdi Masnoddin, Clemente Michael Wong Vui Ling and Nur Athirah Yusof
Microorganisms 2022, 10(8), 1654; https://doi.org/10.3390/microorganisms10081654 - 16 Aug 2022
Cited by 1 | Viewed by 2252
Abstract
Pedobacter cryoconitis BG5 is an obligate psychrophilic bacterium that was first isolated on King George Island, Antarctica. Over the last 50 years, the West Antarctic, including King George Island, has been one of the most rapidly warming places on Earth, hence making it [...] Read more.
Pedobacter cryoconitis BG5 is an obligate psychrophilic bacterium that was first isolated on King George Island, Antarctica. Over the last 50 years, the West Antarctic, including King George Island, has been one of the most rapidly warming places on Earth, hence making it an excellent area to measure the resilience of living species in warmed areas exposed to the constantly changing environment due to climate change. This bacterium encodes a genome of approximately 5694 protein-coding genes. However, 35% of the gene models for this species are found to be hypothetical proteins (HP). In this study, three conserved HP genes of P. cryoconitis, designated pcbg5hp1, pcbg5hp2 and pcbg5hp12, were cloned and the proteins were expressed, purified and their functions and structures were evaluated. Real-time quantitative PCR analysis revealed that these genes were expressed constitutively, suggesting a potentially important role where the expression of these genes under an almost constant demand might have some regulatory functions in thermal stress tolerance. Functional analysis showed that these proteins maintained their activities at low and moderate temperatures. Meanwhile, a low citrate synthase aggregation at 43 °C in the presence of PCBG5HP1 suggested the characteristics of chaperone activity. Furthermore, our comparative structural analysis demonstrated that the HPs exhibited cold-adapted traits, most notably increased flexibility in their 3D structures compared to their counterparts. Concurrently, the presence of a disulphide bridge and aromatic clusters was attributed to PCBG5HP1’s unusual protein stability and chaperone activity. Thus, this suggested that the HPs examined in this study acquired strategies to maintain a balance between molecular stability and structural flexibility. Conclusively, this study has established the structure–function relationships of the HPs produced by P. cryoconitis and provided crucial experimental evidence indicating their importance in thermal stress response. Full article
(This article belongs to the Special Issue Extremophilic Microorganisms and Their Communities)
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13 pages, 1339 KiB  
Review
Challenges in Expression and Purification of Functional Fab Fragments in E. coli: Current Strategies and Perspectives
by Rucha S. Patil, Anupa Anupa, Jaya A. Gupta and Anurag S. Rathore
Fermentation 2022, 8(4), 175; https://doi.org/10.3390/fermentation8040175 - 9 Apr 2022
Cited by 16 | Viewed by 7237
Abstract
Microbial host systems remain the most efficient and cost-effective chassis for biotherapeutics production. Escherichia coli is often the preferred host due to ease of cloning, scale-up, high product yields, and most importantly, cost-effective cultivation. E. coli often experience difficulties in producing biologically active [...] Read more.
Microbial host systems remain the most efficient and cost-effective chassis for biotherapeutics production. Escherichia coli is often the preferred host due to ease of cloning, scale-up, high product yields, and most importantly, cost-effective cultivation. E. coli often experience difficulties in producing biologically active therapeutics such as Fab fragments, which require protein folding and subsequent three-dimensional structure development. This paper outlines the recent improvements in upstream and downstream unit operations for producing Fab fragments in E. coli. Monoclonal antibody fragments (Fab) are a rising class of biotherapeutics and their production has been optimised using coexpression of molecular chaperones such as DsbC or DnaK–DnaJ–GrpE, as well as strain engineering for post-translational modifications such as disulphide bridging. Different media systems such as EnBase and combining nitrogen source supplementation with low-temperature cultivation have resulted in improvement in cell integrity, protein expression, and protein refolding. The recovery of native proteins from insoluble inclusion bodies can be improved by adjusting refolding conditions, as well as by incorporating multimodal and affinity chromatography for achieving high product yields in purification. Recent developments summarised in this review may tune the E. coli expression system to produce more complex and glycosylated proteins for therapeutic use in the near future. Full article
(This article belongs to the Special Issue Process Intensification in Microbial Biotechnology)
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18 pages, 2185 KiB  
Article
Chemical Synthesis of a Functional Fluorescent-Tagged α-Bungarotoxin
by Oliver Brun, Claude Zoukimian, Barbara Oliveira-Mendes, Jérôme Montnach, Benjamin Lauzier, Michel Ronjat, Rémy Béroud, Frédéric Lesage, Didier Boturyn and Michel De Waard
Toxins 2022, 14(2), 79; https://doi.org/10.3390/toxins14020079 - 21 Jan 2022
Cited by 8 | Viewed by 4825
Abstract
α-bungarotoxin is a large, 74 amino acid toxin containing five disulphide bridges, initially identified in the venom of Bungarus multicinctus snake. Like most large toxins, chemical synthesis of α-bungarotoxin is challenging, explaining why all previous reports use purified or recombinant α-bungarotoxin. However, only [...] Read more.
α-bungarotoxin is a large, 74 amino acid toxin containing five disulphide bridges, initially identified in the venom of Bungarus multicinctus snake. Like most large toxins, chemical synthesis of α-bungarotoxin is challenging, explaining why all previous reports use purified or recombinant α-bungarotoxin. However, only chemical synthesis allows easy insertion of non-natural amino acids or new chemical functionalities. Herein, we describe a procedure for the chemical synthesis of a fluorescent-tagged α-bungarotoxin. The full-length peptide was designed to include an alkyne function at the amino-terminus through the addition of a pentynoic acid linker. Chemical synthesis of α-bungarotoxin requires hydrazide-based coupling of three peptide fragments in successive steps. After completion of the oxidative folding, an azide-modified Cy5 fluorophore was coupled by click chemistry onto the toxin. Next, we determined the efficacy of the fluorescent-tagged α-bungarotoxin to block acetylcholine (ACh)-mediated currents in response to muscle nicotinic receptor activation in TE671 cells. Using automated patch-clamp recordings, we demonstrate that fluorescent synthetic α-bungarotoxin has the expected nanomolar affinity for the nicotinic receptor. The blocking effect of fluorescent α-bungarotoxin could be displaced by incubation with a 20-mer peptide mimicking the α-bungarotoxin binding site. In addition, TE671 cells could be labelled with fluorescent toxin, as witnessed by confocal microscopy, and this labelling was partially displaced by the 20-mer competitive peptide. We thus demonstrate that synthetic fluorescent-tagged α-bungarotoxin preserves excellent properties for binding onto muscle nicotinic receptors. Full article
(This article belongs to the Special Issue Toxins: Mr Hyde or Dr Jekyll?)
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13 pages, 5949 KiB  
Article
Poultry Feather Waste as Bio-Based Cross-Linking Additive for Ethylene Propylene Diene Rubber
by Markus Brenner and Oliver Weichold
Polymers 2021, 13(22), 3908; https://doi.org/10.3390/polym13223908 - 12 Nov 2021
Cited by 2 | Viewed by 2687
Abstract
Most rubbers used today rely on sulphur as a cross-linking agent and carbon black from fossil resources to modify the mechanical properties. A very promising substitute can be found in natural keratins such as feathers. These are not only tough, but also contain [...] Read more.
Most rubbers used today rely on sulphur as a cross-linking agent and carbon black from fossil resources to modify the mechanical properties. A very promising substitute can be found in natural keratins such as feathers. These are not only tough, but also contain a relevant amount of sulphur in the form of disulphide bridges. The present study shows that these can be activated under vulcanisation conditions and then bind covalently to EPDM rubber to form a cross-linked network. Feathers were cut into lengths of 0.08, 0.2, and 1 mm and incorporated at 38, 69, or 100 phr into EPDM mixtures containing either no carbon black or no carbon black nor sulphur. The presence of feather cuttings increases the tensile and compressive strength as well as the hardness, and reduces the rebound resilience. Due to their high (approximately 17%) nitrogen content, the feathers also improve the thermal stability of the composite, as the main degradation step is shifted from 400 °C to 470 °C and the decomposition is significantly slowed down. Since elastomers are a large market and feathers in particular are a high-volume waste, the combination of these two offers enormous ecological and economic prospects. Full article
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23 pages, 19188 KiB  
Article
Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates
by Michele Di Foggia, Masuhiro Tsukada and Paola Taddei
Molecules 2021, 26(21), 6487; https://doi.org/10.3390/molecules26216487 - 27 Oct 2021
Cited by 2 | Viewed by 2614
Abstract
In the last decades, silk fibroin and wool keratin have been considered functional materials for biomedical applications. In this study, fabrics containing silk fibers from Bombyx mori and Tussah silk fibers from Antheraea pernyi, as well as wool keratin fabrics, were grafted [...] Read more.
In the last decades, silk fibroin and wool keratin have been considered functional materials for biomedical applications. In this study, fabrics containing silk fibers from Bombyx mori and Tussah silk fibers from Antheraea pernyi, as well as wool keratin fabrics, were grafted with phosmer CL and phosmer M (commercial names, i.e., methacrylate monomers containing phosphate groups in the molecular side chain) with different weight gains. Both phosmers were recently proposed as flame retarding agents, and their chemical composition suggested a possible application in bone tissue engineering. IR and Raman spectroscopy were used to disclose the possible structural changes induced by grafting and identify the most reactive amino acids towards the phosmers. The same techniques were used to investigate the nucleation of a calcium phosphate phase on the surface of the samples (i.e., bioactivity) after ageing in simulated body fluid (SBF). The phosmers were found to polymerize onto the biopolymers efficiently, and tyrosine and serine underwent phosphorylation (monitored through the strengthening of the Raman band at 1600 cm−1 and the weakening of the Raman band at 1400 cm−1, respectively). In grafted wool keratin, cysteic acid and other oxidation products of disulphide bridges were detected together with sulphated residues. Only slight conformational changes were observed upon grafting, generally towards an enrichment in ordered domains, suggesting that the amorphous regions were more prone to react (and, sometimes, degrade). All samples were shown to be bioactive, with a weight gain of up to 8%. The most bioactive samples contained the highest phosmers amounts, i.e., the highest amounts of phosphate nucleating sites. The sulphate/sulphonate groups present in grafted wool samples appeared to increase bioactivity, as shown by the five-fold increase of the IR phosphate band at 1040 cm−1. Full article
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14 pages, 2715 KiB  
Article
Autogenous Cross-Linking of Recycled Keratin from Poultry-Feather Waste to Hydrogels for Plant-Growth Media
by Markus Brenner and Oliver Weichold
Polymers 2021, 13(20), 3581; https://doi.org/10.3390/polym13203581 - 17 Oct 2021
Cited by 9 | Viewed by 3085
Abstract
The global rise in atmospheric temperature is leading to an increasing spread of semi-arid and arid regions and is accompanied by a deterioration of arable land. Polymers can help in a number of ways, but they must not be a burden to the [...] Read more.
The global rise in atmospheric temperature is leading to an increasing spread of semi-arid and arid regions and is accompanied by a deterioration of arable land. Polymers can help in a number of ways, but they must not be a burden to the environment. In this context, we present herein a method by which goose feathers, representative of keratin waste in general, can be transformed into hydrogels for use as a plant growth medium. The treatment of shredded feathers in Na2S solution at ambient conditions dissolves approx. 80% of the keratin within 30 min. During evaporation, the thiol groups of cysteine reoxidise to disulphide bridges. Additionally, the protein chains form β-sheets. Both act as cross-links that enables the formation of gels. The drying conditions were found to be crucial as slower evaporation affords gels with higher degrees of swelling at the cost of reduced gel yields. The cress germination test indicated the absence of toxic substances in the gel, which strongly adheres to the roots. Thereby, the plants are protected from drought stress as long as the gel still contains moisture. Full article
(This article belongs to the Special Issue Polymers for Soil in Agriculture and Urban Landscaping)
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11 pages, 4418 KiB  
Article
A Cyclic BMP-2 Peptide Upregulates BMP-2 Protein-Induced Cell Signaling in Myogenic Cells
by Vijaya Narasimha Gudivada, Chen-Ji Huang, Yueh-Hsia Luo and Guo-Chung Dong
Polymers 2021, 13(15), 2549; https://doi.org/10.3390/polym13152549 - 31 Jul 2021
Cited by 4 | Viewed by 2955
Abstract
In the current study, we designed four cyclic peptide analogues by incorporating two cysteine residues in a BMP-2 linear knuckle epitope in such a way that the active region of the peptide could be either inside or outside the cyclic ring. Bone morphogenetic [...] Read more.
In the current study, we designed four cyclic peptide analogues by incorporating two cysteine residues in a BMP-2 linear knuckle epitope in such a way that the active region of the peptide could be either inside or outside the cyclic ring. Bone morphogenetic protein receptor BMPRII was immobilized on the chip surface, and the interaction of the linear and cyclic peptide analogues was studied using surface plasmon resonance (SPR). From the affinity data, the peptides with an active region inside the cyclic ring had a higher binding affinity in comparison to the other peptides. To confirm that our affinity data are in line in vitro, we studied the expression levels of RUNX2 (runt-related transcription factor) and conducted an osteogenic marker alkaline phosphatase (ALP) assay and staining. Based on the affinity data and the in vitro experiments, peptide P-05 could be a suitable candidate for osteogenesis, with higher binding affinity and increased RUNX2 and ALP expression in comparison to the linear peptides. Full article
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