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New Insights into Bioactive Peptides: Design, Synthesis, Structure-Activity Relationship 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Bioactives and Nutraceuticals".

Deadline for manuscript submissions: 25 November 2024 | Viewed by 270

Special Issue Editors


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Guest Editor
Institute of Biostructures and Bioimaging (IBB), National Research Council of Italy (CNR), Via Mezzocannone 16, 80134 Naples, Italy
Interests: structural biology; NMR; drug discovery; conformational analysis of proteins and peptides; protein–protein interactions (PPIs); design and evaluation of PPI inhibitors; structure-based drug design; molecular modeling; docking; cancer
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
CNR-IBB (National Research Council-Institute of Biostructures and Bioimaging), Via Tommaso De Amicis 95, Naples, Italy
Interests: structural biology; NMR; drug discovery; conformational analysis of proteins and peptides; protein–protein interactions (PPIs); design and evaluation of PPI inhibitors; structure-based drug design; molecular modeling; docking
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Peptides consist of amino acids linked by covalent bonds similarly to proteins but with a shorter chain. Synthetic and natural peptides may hold interesting biological functions and consequently they have aroused increasing attention in drug design/drug discovery research fields. Peptide sequences may reflect proteins spots responsible for molecular recognition and biological activities, thus can act as enzyme inhibitors or protein-protein interaction modulators and interfere with signaling pathways. Peptides may possess therapeutic potential and be employed to set-up original therapies in alternative to small molecules and protein drugs due to their unique features of potency, specificity, and low toxicity profile. Since the discovery of Insulin for diabetes treatment, peptide drugs have been implemented to treat a wide range of diseases, including cancer, osteoporosis, multiple sclerosis, HIV infection and chronic pain. Moreover, peptides can play a supporting role in disease diagnosis and drug delivery. As peptides may be affected by high protease sensitivity and defective pharmacokinetics, different chemical strategies have been proposed for overcoming these issues, such as peptide stapling and cyclization and peptidomimetics design. Several computational tools have been also devoted to peptide ligand design and screening against biological macromolecular targets, and peptide structure manipulation.

The present Special Issue aims to cover the above-described topics by means of contributions (communication, full papers and reviews) particularly focused on innovative experimental and computational approaches towards the development of bioactive peptides.

Dr. Marilisa Leone
Dr. Flavia Anna Mercurio
Guest Editors

Manuscript Submission Information

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Keywords

  • peptides
  • protein-peptide interactions
  • PPI inhibition and modulation
  • peptide drugs
  • peptidomimetics
  • cyclic peptides
  • stapled peptides
  • diagnostic peptides
  • peptides for drug delivery
  • multidisciplinary approaches

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Published Papers (1 paper)

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Research

10 pages, 12079 KiB  
Communication
Subtle Structural Differences Affect the Inhibitory Potency of RGD-Containing Cyclic Peptide Inhibitors Targeting SPSB Proteins
by Kefa Li, Yanhong Luo, Weiwei Hu, Jinjin Yang, Danting Zhang, Huan Wei, Tingting You, Hai-Shu Lin and Zhihe Kuang
Int. J. Mol. Sci. 2024, 25(12), 6764; https://doi.org/10.3390/ijms25126764 - 20 Jun 2024
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Abstract
The SPRY domain-containing SOCS box proteins SPSB1, SPSB2, and SPSB4 utilize their SPRY/B30.2 domain to interact with a short region in the N-terminus of inducible nitric oxide synthase (iNOS), and recruit an E3 ubiquitin ligase complex to polyubiquitinate iNOS, resulting in the proteasomal [...] Read more.
The SPRY domain-containing SOCS box proteins SPSB1, SPSB2, and SPSB4 utilize their SPRY/B30.2 domain to interact with a short region in the N-terminus of inducible nitric oxide synthase (iNOS), and recruit an E3 ubiquitin ligase complex to polyubiquitinate iNOS, resulting in the proteasomal degradation of iNOS. Inhibitors that can disrupt the endogenous SPSB-iNOS interactions could be used to augment cellular NO production, and may have antimicrobial and anticancer activities. We previously reported the rational design of a cyclic peptide inhibitor, cR8, cyclo(RGDINNNV), which bound to SPSB2 with moderate affinity. We, therefore, sought to develop SPSB inhibitors with higher affinity. Here, we show that cyclic peptides cR7, cyclo(RGDINNN), and cR9, cyclo(RGDINNNVE), have ~6.5-fold and ~2-fold, respectively, higher SPSB2-bindng affinities than cR8. We determined high-resolution crystal structures of the SPSB2-cR7 and SPSB2-cR9 complexes, which enabled a good understanding of the structure–activity relationships for these cyclic peptide inhibitors. Moreover, we show that these cyclic peptides displace full-length iNOS from SPSB2, SPSB1, and SPSB4, and that their inhibitory potencies correlate well with their SPSB2-binding affinities. The strongest inhibition was observed for cR7 against all three iNOS-binding SPSB proteins. Full article
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