AI Article Synopsis
- Host defense peptides (AMPs) are short amino acid sequences known for their broad-spectrum antimicrobial properties against bacteria, viruses, and fungi, which can be pivotal for developing new antibiotics.
- Many researchers have identified that AMPs rich in tryptophan, arginine, and proline show promising potential as next-generation antibiotics, prompting further exploration of these specific sequences.
- In the study, 2924 AMPs were analyzed based on their sources, structures, and activities, focusing on those with high concentrations of the targeted amino acids and utilizing molecular modeling and simulations to assess their stability and structure.
Article Abstract
The host defense peptides or antimicrobial peptides (AMPs) often contain short sequence of amino acids, either positive or negatively charged and express broad-spectrum antibacterial, antiviral and antifungal activity. Many researchers had reported that tryptophan, arginine and proline rich AMPs have a promising source of next-generation antibiotics. Nowadays, AMPs are used as a possible therapeutic source for future antibiotics. In the present study, the amino acid sequences of 2924 AMPs belonging to various sources rich in Tryptophan, Proline and Arginine was chosen for investigation. The AMPs were further categorized according to their source, structure and antimicrobial activities. The AMPs with tryptophan, arginine, proline residues in abundance with maximum sequence length of 20 amino acids alone was obtained. Homology modeling was performed with PEP-FOLD and the modeled structures were evaluated using RAMPAGE to identify the structural information. Further, the stability of peptide in aqueous condition was probed using molecular dynamics simulations.Communicated by Ramaswamy H. Sarma.
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| http://dx.doi.org/10.1080/07391102.2020.1848631 | DOI Listing |
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