Asset Details
Do you wish to reserve the book?
Proline-Rich Antimicrobial Peptides from Invertebrates
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Proline-Rich Antimicrobial Peptides from Invertebrates
Do you wish to request the book?
Proline-Rich Antimicrobial Peptides from Invertebrates
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Proline-Rich Antimicrobial Peptides from Invertebrates
2024
Overview
Antimicrobial peptides (AMPs) constitute a large and diverse group of molecules with antibacterial, antifungal, antiviral, antiprotozoan, and anticancer activity. In animals, they are key components of innate immunity involved in fighting against various pathogens. Proline-rich (Pr) AMPs are characterized by a high content of proline (and arginine) residues that can be organized into Pro-Arg-Pro motifs. Such peptides have been described in many invertebrates (annelids, crustaceans, insects, mollusks) and some vertebrates (mammals). The main objective of this review is to present the diversity of invertebrate PrAMPs, which are associated with the presence of cysteine-rich domains or whey acidic protein domains in the molecular structure, in addition to the presence of characteristic proline-rich regions. Moreover, PrAMPs can target intracellular structures in bacteria, e.g., 70S ribosomes and/or heat shock protein DnaK, leading to the inhibition of protein synthesis and accumulation of misfolded polypeptides in the cell. This unique mechanism of action makes it difficult for pathogens to acquire resistance to this type of molecule. Invertebrate PrAMPs have become the basis for the development of new synthetic analogues effective in combating pathogens. Due to their great diversity, new highly active molecules are still being searched for among PrAMPs from invertebrates.
Publisher
MDPI AG
Subject
/ Animals
/ Anti-Infective Agents - chemistry
/ Anti-Infective Agents - pharmacology
/ Antimicrobial Cationic Peptides - chemistry
/ Antimicrobial Cationic Peptides - pharmacology
/ Antimicrobial Peptides - chemistry
/ Antimicrobial Peptides - pharmacology
/ Bacteria
/ Cysteine
/ DnaK
/ drosocin
/ Drug resistance in microorganisms
/ Fungi
/ Genes
/ Peptides
/ PrAMP uptake by bacterial cells
/ Proline
/ proline-rich antimicrobial peptides
/ Worms
