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Peptides is a monthly peer-reviewed scientific journal covering the biochemistry, neurochemistry, pharmacology, and biological functions of peptides. It was established in 1980 and is published by Elsevier. The editor-in-chief is Karl-Heinz Herzig (University of Oulu).
The Journal of Peptide Science is abstracted and indexed by Chemical Abstracts Service, MEDLINE/PubMed, Scopus, and the Science Citation Index.According to the Journal Citation Reports, the journal has a 2021impact factor of 2.408, ranking it 66th out of 87 journals in the category "Chemistry Analytical" [1] and 255th out of 297 journals in the category "Biochemistry & Molecular Biology".
There are numerous types of peptides that have been classified according to their sources and functions. According to the Handbook of Biologically Active Peptides, some groups of peptides include plant peptides, bacterial/antibiotic peptides, fungal peptides, invertebrate peptides, amphibian/skin peptides, venom peptides, cancer/anticancer peptides, vaccine peptides, immune/inflammatory ...
Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms. [1] While there exist a wide range of peptides that are not synthesized by ribosomes, the term nonribosomal peptide typically refers to a very specific set of these as discussed in this article.
Biological Chemistry (journal) Biological Trace Element Research; Biomacromolecules; Biomarker Insights; Biomarkers (journal) Biomarkers in Medicine; Biomaterials Science; Biomedical Chromatography; BioMetals (journal) Biomolecules (journal) Bioorganic & Medicinal Chemistry; Bioorganic & Medicinal Chemistry Letters; Biopolymers (journal)
These studies led to the need for peptide synthesis and, eventually, to the idea for solid phase peptide synthesis (SPPS) in 1959. In 1963, he was sole author of a classic paper in the Journal of the American Chemical Society in which he reported a method he called "solid phase peptide synthesis". [ 4 ]
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
Proposed mechanism of peptide cleavage by aspartyl proteases. [6]Aspartyl proteases are a highly specific family of proteases – they tend to cleave dipeptide bonds that have hydrophobic residues as well as a beta-methylene group.