Antimicrobial peptides (AMPs) are gaining popularity as anti-infective agents. Information on sequence features that contribute to target specificity of AMPs will aid in accelerating drug discovery programs involving them. In this study, an algorithm called ClassAMP using Random Forests (RFs) and Support Vector Machines (SVMs) has been developed to predict the propensity of a protein sequence to have antibacterial, antifungal, or antiviral activity. ClassAMP is available at http://www.bicnirrh.res.in/classamp/.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1109/TCBB.2012.89 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Novel Leech Antimicrobial Peptides, Hirunipins: Real-Time 3D Monitoring of Antimicrobial and Antibiofilm Mechanisms Using Optical Diffraction Tomography.
Adv Sci (Weinh)
January 2025
Department of Biological Sciences and Biotechnology, College of Natural Sciences, Chungbuk National University, Cheongju, Chungbuk, 28644, Republic of Korea.
Antimicrobial peptides (AMPs) are promising agents for treating antibiotic-resistant bacterial infections. Although discovering novel AMPs is crucial for combating multidrug-resistant bacteria and biofilm-related infections, their clinical potential relies on precise, real-time evaluation of efficacy, toxicity, and mechanisms. Optical diffraction tomography (ODT), a label-free imaging technology, enables real-time visualization of bacterial morphological changes, membrane damage, and biofilm formation over time.
View Article and Find Full Text PDFdeep-AMPpred: A Deep Learning Method for Identifying Antimicrobial Peptides and Their Functional Activities.
J Chem Inf Model
January 2025
School of Information and Artificial Intelligence, Anhui Provincial Engineering Research Center for Beidou Precision Agriculture Information, Key Laboratory of Agricultural Sensors for Ministry of Agriculture and Rural Affairs, Anhui Agricultural University, Hefei, Anhui 230036, China.
Antimicrobial peptides (AMPs) are small peptides that play an important role in disease defense. As the problem of pathogen resistance caused by the misuse of antibiotics intensifies, the identification of AMPs as alternatives to antibiotics has become a hot topic. Accurately identifying AMPs using computational methods has been a key issue in the field of bioinformatics in recent years.
View Article and Find Full Text PDFEffect of Chirality and Amphiphilicity on the Antimicrobial Activity of Tripodal Lysine-Based Peptides.
ACS Appl Bio Mater
January 2025
School of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading RG6 6AD, U.K.
A series of tripodal (three-arm) lysine-based peptides were designed and synthesized and their self-assembly properties in aqueous solution and antimicrobial activity were investigated. We compare the behaviors of homochiral tripodal peptides (KKY)K and a homologue containing the bulky aromatic fluorenylmethoxycarbonyl (Fmoc) group Fmoc-(KKY)K, and heterochiral analogues containing k (d-Lys), (kkY)K and Fmoc-(kkY)K. The molecular conformation and self-assembly in aqueous solutions were probed using various spectroscopic techniques, along with small-angle X-ray scattering (SAXS) and cryogenic-transmission electron microscopy (cryo-TEM).
View Article and Find Full Text PDFAmphibian-Derived Antimicrobial Peptides: Essential Components of Innate Immunity and Potential Leads for New Antibiotic Development.
Protein Pept Lett
January 2025
Department of Biology, Faculty of Science, Ege University, Izmir, Turkey.
Like other vertebrates, amphibians possess innate and adaptive immune systems. At the center of the adaptive immune system is the Major Histocompatibility Complex. The important molecules of innate immunity are antimicrobial peptides (AMPs).
View Article and Find Full Text PDFImproving the antimicrobial potential of the peptide CIDEM-501 through acylation: A computational approach.
Biochim Biophys Acta Biomembr
January 2025
Biochemistry and Molecular Biology Department, Center for Pharmaceutical Research and Development, Ave. 26 # 1605, Nuevo Vedado, Ciudad de La Habana, 10400, Cuba. Electronic address:
Acylation is a common method used to modify antimicrobial peptides to enhance their effectiveness. It increases the interactions between the peptide and the bacterial cell membranes. However, acylation can also reduce the selectivity of the peptides by making them more active on eukaryotic membranes, which can lead to unintended toxicity.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!