The ongoing search for effective treatment of Acne vulgaris is concentrated, i.a., on natural peptides with antimicrobial properties. The aim of this work was the development of new amino acid derivatives with potential activity on dermal infections against selected microorganisms, including the facultative anaerobe . The peptides P1-P6 were synthesized via Fmoc solid phase peptide synthesis using Rink amide AM resin, analyzed by RP-HPLC-MS, FTIR, DPPH radical scavenging activity, and evaluated against and , both deposited and non-deposited in BC. Peptides P1-P6 presented a lack of cytotoxicity, antimicrobial activity, or antioxidative properties correlated with selected structural properties. P2 and P4-P6 sorption in BC resulted in variable data, i.a., confirming the prospective topical application of these peptides in a BC carrier.
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http://dx.doi.org/10.3390/ijms22147466 | DOI Listing |
Int J Mol Sci
December 2024
Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture (CAS), Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266000, China.
Marine microalgae are a rich source of natural products, and their amino acid-based antimicrobial agents are usually obtained by enzymatic hydrolysis, which is inefficient and limits the research on antimicrobial peptides (AMPs) from microalgae. In this study, is used as a model to predict antimicrobial peptides through high-throughput methods, and 471 putative peptides are identified based on the de novo transcriptome technique. Among them, three short peptides, P1, P6, and P7 were found to have antimicrobial activity against , , , and yeast , and they showed no hemolytic activity even at higher concentrations up to 10 mg/mL.
View Article and Find Full Text PDFACS Nano
November 2024
Department of Chemistry, Haverford College, Haverford, Pennsylvania 19041, United States.
A peptide corresponding to a 13-residue segment of the human protein semenogelin I has been shown to generate a hydrogel consisting of amyloid-like fibrils. The relative chemical diversity (compared to synthetic sequences) with 11 distinct amino acids makes this peptide (P0) an ideal candidate for investigating the role of individual residues in gelation. Herein, the terminal residues have been sequentially removed to furnish a series of truncated peptides, P1-P10, ranging from 12 to 3 residues in length.
View Article and Find Full Text PDFChemistry
August 2024
Organic & Medicinal Chemistry Division, Indian Institute of Chemical Biology (CSIR-IICB), 4-Raja S. C. Mullick Road, Kolkata, 700032, India.
Cyclic dipeptides (CDPs) are crucial building blocks for a range of functional nanomaterials due to their simple chemical structure and high molecular stability. In this investigation, we synthesized a set of S-benzyl-L-cysteine-based CDPs (designated as P1-P6) and thoroughly examined their self-assembly behavior in a methanol-water solvent to elucidate the relationship between their structure and gelation properties. The hydrophobicity of the amino acids within the CDPs was gradually increased.
View Article and Find Full Text PDFFoods
August 2022
College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, China.
Antioxidants, which can activate the body's antioxidant defence system and reduce oxidative stress damage, are important for maintaining free radical homeostasis between oxidative damage and antioxidant defence. Six antioxidant peptides (P1-P6) were isolated and identified from the enzymatic hydrolysate of tilapia skin by ultrafiltration, reversed-phase high-performance liquid chromatography (RP-HPLC) and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Moreover, the scavenging mechanism of the identified peptides against DPPH (2,2-Diphenyl-1-picrylhydrazyl) and ABTS (2-azido-bis (3-ethylbenzothiazoline-6-sulfonic acid) was studied by molecular docking.
View Article and Find Full Text PDFProtein Sci
July 2022
Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
The infectivity of HIV-1 requires its protease (PR) cleave multiple cut-sites with low sequence similarity. The diversity of cleavage sites has made it challenging to investigate the underlying sequence properties that determine binding and turnover of substrates by PR. We engineered a mutational scanning approach utilizing yeast display, flow cytometry, and deep sequencing to systematically measure the impacts of all individual amino acid changes at 12 positions in three different cut-sites (MA/CA, NC/p1, and p1/p6).
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