Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
7.8
5.6
Journals
IJMS
Special Issues
New Trend in the Research of Short Peptides
ijms-logo
Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

New Trend in the Research of Short Peptides

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

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 4971

Special Issue Editor

Prof. Dr. Natalia Linkova

E-Mail Website
Guest Editor
1. Department of Biogerontology, Saint Petersburg Institute of Bioregulation and Gerontology, 197110 Saint Petersburg, Russia
2. The Department of Therapy, Geriatrics and Anti-Age Medicine, Academy of Postgraduate Education under of FSBU FSCC of FMBA of Russia, 125371 Moscow, Russia
3. The Laboratory “Problems of Aging”, Belgorod National Research University, 308015 Belgorod, Russia
Interests: peptide drugs; bioinformatic; cell aging; predictive diagnostic of age-related diseases; immunology; neurobiology

Special Issue Information

Dear Colleagues,

Peptides have the wide range of biological and physological activity. They regulate functions of antioxidant, endocrine, nervous, immune and other systems in humans and animals. The mechanism of peptides activity involves their ability to regulate gene expression and protein synthesis. Peptides can regulate cell differentiation, proliferation, apoptosis and senescence. Drugs on the base of peptides include short peptides (2-8 amino acids residues) and polypeptides. This Special Issue is devoted to a wide range of issues of peptide bioregulation. It includes theoretical studies should offer new insights into the understanding of peptide bioregulation, clinical and experimental results or suggest new testable hypotheses of physiological, geroprotective and theraupeutic role of peptides. This Special issue can include the describtion of molecular mechanisms of peptide activity, DNA-peptide interaction, peptide transpotr into the cell, peptide pharmacokinetic, investigation of peptide activity in cellular, organs and organisms level of human and animals. 

Prof. Dr. Natalia Linkova
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • short peptides
  • polypeptides
  • biological activity
  • peptides drug
  • cellular senescence
  • neuroprotection
  • immunoprotection
  • molecular modelling
  • peptide transport
  • peptide regulation of gene expression

Published Papers (3 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

17 pages, 2400 KiB  
Article
Phosphorylated Peptide Derived from the Myosin Phosphatase Target Subunit Is a Novel Inhibitor of Protein Phosphatase-1
by Zoltán Kónya, István Tamás, Bálint Bécsi, Beáta Lontay, Mária Raics, István Timári, Katalin E. Kövér and Ferenc Erdődi
Int. J. Mol. Sci. 2023, 24(5), 4789; https://doi.org/10.3390/ijms24054789 - 01 Mar 2023
Viewed by 1330
Abstract
Identification of specific protein phosphatase-1 (PP1) inhibitors is of special importance regarding the study of its cellular functions and may have therapeutic values in diseases coupled to signaling processes. In this study, we prove that a phosphorylated peptide of the inhibitory region of [...] Read more.
Identification of specific protein phosphatase-1 (PP1) inhibitors is of special importance regarding the study of its cellular functions and may have therapeutic values in diseases coupled to signaling processes. In this study, we prove that a phosphorylated peptide of the inhibitory region of myosin phosphatase (MP) target subunit (MYPT1), R690QSRRS(pT696)QGVTL701 (P-Thr696-MYPT1690−701), interacts with and inhibits the PP1 catalytic subunit (PP1c, IC50 = 3.84 µM) and the MP holoenzyme (Flag-MYPT1-PP1c, IC50 = 3.84 µM). Saturation transfer difference NMR measurements established binding of hydrophobic and basic regions of P-Thr696-MYPT1690−701 to PP1c, suggesting interactions with the hydrophobic and acidic substrate binding grooves. P-Thr696-MYPT1690−701 was dephosphorylated by PP1c slowly (t1/2 = 81.6–87.9 min), which was further impeded (t1/2 = 103 min) in the presence of the phosphorylated 20 kDa myosin light chain (P-MLC20). In contrast, P-Thr696-MYPT1690−701 (10–500 µM) slowed down the dephosphorylation of P-MLC20 (t1/2 = 1.69 min) significantly (t1/2 = 2.49–10.06 min). These data are compatible with an unfair competition mechanism between the inhibitory phosphopeptide and the phosphosubstrate. Docking simulations of the PP1c-P-MYPT1690−701 complexes with phosphothreonine (PP1c-P-Thr696-MYPT1690−701) or phosphoserine (PP1c-P-Ser696-MYPT1690−701) suggested their distinct poses on the surface of PP1c. In addition, the arrangements and distances of the surrounding coordinating residues of PP1c around the phosphothreonine or phosphoserine at the active site were distinct, which may account for their different hydrolysis rate. It is presumed that P-Thr696-MYPT1690−701 binds tightly at the active center but the phosphoester hydrolysis is less preferable compared to P-Ser696-MYPT1690−701 or phosphoserine substrates. Moreover, the inhibitory phosphopeptide may serve as a template to synthesize cell permeable PP1-specific peptide inhibitors. Full article
(This article belongs to the Special Issue New Trend in the Research of Short Peptides)
►▼ Show Figures

Figure 1

Review

Jump to: Research

14 pages, 1338 KiB  
Review
Advancement from Small Peptide Pharmaceuticals to Orally Active Piperazine-2,5-dion-Based Cyclopeptides
by Vladislav Deigin, Natalia Linkova and Olga Volpina
Int. J. Mol. Sci. 2023, 24(17), 13534; https://doi.org/10.3390/ijms241713534 - 31 Aug 2023
Viewed by 1072
Abstract
The oral delivery of peptide pharmaceuticals has long been a fundamental challenge in drug development. A new chemical platform was designed based on branched piperazine-2,5-diones for creating orally available biologically active peptidomimetics. The platform includes a bio-carrier with “built-in” functionally active peptide fragments [...] Read more.
The oral delivery of peptide pharmaceuticals has long been a fundamental challenge in drug development. A new chemical platform was designed based on branched piperazine-2,5-diones for creating orally available biologically active peptidomimetics. The platform includes a bio-carrier with “built-in” functionally active peptide fragments or bioactive molecules that are covalently attached via linkers. The developed platform allows for a small peptide to be taken with a particular biological activity and to be transformed into an orally stable compound displaying the same activity. Based on this approach, various peptidomimetics exhibiting hemostimulating, hemosuppressing, and adjuvant activity were prepared. In addition, new examples of a rare phenomenon when enantiomeric molecules demonstrate reciprocal biological activity are presented. Finally, the review summarizes the evolutionary approach of the short peptide pharmaceutical development from the immunocompetent organ separation to orally active cyclopeptides and peptidomimetics. Full article
(This article belongs to the Special Issue New Trend in the Research of Short Peptides)
►▼ Show Figures

Figure 1

13 pages, 954 KiB  
Review
Peptide Regulation of Chondrogenic Stem Cell Differentiation
by Natalia Linkova, Vladimir Khavinson, Anastasiia Diatlova, Svetlana Myakisheva and Galina Ryzhak
Int. J. Mol. Sci. 2023, 24(9), 8415; https://doi.org/10.3390/ijms24098415 - 08 May 2023
Viewed by 1785
Abstract
The search for innovative ways to treat osteoarthritis (OA) is an urgent task for molecular medicine and biogerontology. OA leads to disability in persons of middle and older age, while safe and effective methods of treating OA have not yet been discovered. The [...] Read more.
The search for innovative ways to treat osteoarthritis (OA) is an urgent task for molecular medicine and biogerontology. OA leads to disability in persons of middle and older age, while safe and effective methods of treating OA have not yet been discovered. The directed differentiation of mesenchymal stem cells (MSCs) into chondrocytes is considered one of the possible methods to treat OA. This review describes the main molecules involved in the chondrogenic differentiation of MSCs. The peptides synthesized on the basis of growth factors’ structures (SK2.1, BMP, B2A, and SSPEPS) and components of the extracellular matrix of cartilage tissue (LPP, CFOGER, CMP, RDG, and N-cadherin mimetic peptide) offer the greatest promise for the regulation of the chondrogenic differentiation of MSCs. These peptides regulate the WNT, ERK-p38, and Smad 1/5/8 signaling pathways, gene expression, and the synthesis of chondrogenic differentiation proteins such as COL2, SOX9, ACAN, etc. Full article
(This article belongs to the Special Issue New Trend in the Research of Short Peptides)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-3
Back to TopTop