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Special Issue Editor

Prof. Dr. Reinhard Schweitzer-Stenner

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Guest Editor

Department of Chemistry, Drexel University, Philadelphia, PA 19104, USA
Interests: vibrational spectroscopy (raman, IR, vibrational circular dichroism); structure analysis of unfolded peptides; self-assembly and gelation of short and ultrashort peptides; structure and function of heme proteins

Special Issue Information

Dear Colleagues,

The special issue on peptide gelation will provide a compendium of different experimental and computational approaches aimed at understanding the rules which govern the self-assembly and gelation of short peptides. A mixture of review, perspective and original research articles will inform the reader about the design strategies, criteria for peptide self-assembly and gelation, the relationship between peptide chemistry, fibril length and gel strength explored by microscopic and rheological techniques. Some studies will focus on how solution conditions, solvent composition and concentration affect the kinetics of gel formation, the respective fibril network, the strength of the gel phase and its stability. Some papers will demonstrate how optical and vibrational spectroscopy can be used to obtain information about the structure of the fibrils that underlie the gel phases of short peptides. While most of the papers will focus on the structural and mechanism issue, possible biomedical applications of peptide gels will be described as well.

Prof. Dr. Reinhard Schweitzer-Stenner
Guest Editor

Manuscript Submission Information

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Keywords

self-assembly of peptides in various solvents
peptide gelation, gelation and peptide solubility
peptide chemistry
spectroscopy on peptide gels
gelation kinetics

Published Papers (2 papers)

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Research

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17 pages, 8028 KiB

Open AccessArticle

Effect of Newly Synthesized Structures of Peptides on the Stability of the Monolayers Formed

by Iwona Golonka, Katarzyna E. Greber, Bartłomiej M. Szyja, Patrycja P. Petrus, Jakub E. Pucułek and Witold Musiał

Int. J. Mol. Sci. 2023, 24(5), 4318; https://doi.org/10.3390/ijms24054318 - 21 Feb 2023

Cited by 3 | Viewed by 1473

Abstract

The aim of the study was to evaluate the effect of the peptide structure (WKWK)₂-KWKWK-NH₂, P4 (C12)₂-KKKK-NH₂, P5 (KWK)₂-KWWW-NH₂, P6 (KK)₂-KWWW-NH₂ on their physicochemical properties. The thermogravimetric method (TG/DTG) was used, which made it possible to observe the course of chemical reactions and phase transformations occurring during the heating of solid samples. Based on the DSC curves, the enthalpy of the processes occurring in the peptides was determined. The influence of the chemical structure of this group of compounds on their film-forming properties was determined using the Langmuir–Wilhelmy trough method and was followed by molecular dynamics simulation. Evaluated peptides showed high thermal stability and the first significant mass loss occurred only at about 230 °C and 350 °C. The analysis of the compressibility coefficient of individual peptides indicates that all formed peptide monolayers were in the expanded liquid phase. Their maximum compressibility factor was less than 50.0 mN/m. Its highest value of 42.7 mN/m was achieved in a monolayer made of P4. The results obtained in molecular dynamic simulation indicate that non-polar side chains played an important role in the properties of the P4 monolayer, and the same applies to P5, except that a spherical effect was observed here. A slightly different behavior was observed for the P6 and P2 peptide systems, where the type of amino acids present had an influence. The obtained results indicate that the structure of the peptide affected its physicochemical and layer-forming properties. Full article

(This article belongs to the Special Issue Self-Assembly and Gelation of Short and Ultrashort Peptides)

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Review

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27 pages, 3342 KiB

Open AccessReview

Peptide- and Metabolite-Based Hydrogels: Minimalistic Approach for the Identification and Characterization of Gelating Building Blocks

by Om Shanker Tiwari, Sigal Rencus-Lazar and Ehud Gazit

Int. J. Mol. Sci. 2023, 24(12), 10330; https://doi.org/10.3390/ijms241210330 - 19 Jun 2023

Cited by 3 | Viewed by 1606

Abstract

Minimalistic peptide- and metabolite-based supramolecular hydrogels have great potential relative to traditional polymeric hydrogels in various biomedical and technological applications. Advantages such as remarkable biodegradability, high water content, favorable mechanical properties, biocompatibility, self-healing, synthetic feasibility, low cost, easy design, biological function, remarkable injectability, and multi-responsiveness to external stimuli make supramolecular hydrogels promising candidates for drug delivery, tissue engineering, tissue regeneration, and wound healing. Non-covalent interactions such as hydrogen bonding, hydrophobic interactions, electrostatic interactions, and π–π stacking interactions play key roles in the formation of peptide- and metabolite-containing low-molecular-weight hydrogels. Peptide- and metabolite-based hydrogels display shear-thinning and immediate recovery behavior due to the involvement of weak non-covalent interactions, making them supreme models for the delivery of drug molecules. In the areas of regenerative medicine, tissue engineering, pre-clinical evaluation, and numerous other biomedical applications, peptide- and metabolite-based hydrogelators with rationally designed architectures have intriguing uses. In this review, we summarize the recent advancements in the field of peptide- and metabolite-based hydrogels, including their modifications using a minimalistic building-blocks approach for various applications. Full article

(This article belongs to the Special Issue Self-Assembly and Gelation of Short and Ultrashort Peptides)

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