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Arsenals of Pharmacotherapeutically Active Proteins and Peptides: Old Wine in a New Bottle
Published in Debarshi Kar Mahapatra, Swati Gokul Talele, Tatiana G. Volova, A. K. Haghi, Biologically Active Natural Products, 2020
On the basis of number of amino acids present, peptides can be classified as: Dipeptide which contains two amino acid residues.Tripeptide which contains three amino acid residues.Tetrapeptide which contains four amino acid residues.Oligopeptides which contain less than 10 amino acid residues.Polypeptides which contain 50 or less than 50 amino acid residues.
Importance of bacterial biodegradation and detoxification processes of microcystins for environmental health
Published in Journal of Toxicology and Environmental Health, Part B, 2018
Isaac Yaw Massey, Xian Zhang, Fei Yang
In the MC-LR biodegradation by Sphingomonas sp. ACM-3962, Bourne et al (1996, 2001) were the first to describe a novel pathway involving 4 genes, 3 intracellular hydrolytic enzymes, and 2 intermediate products. The 3 enzymes were encoded by the gene cluster, sequentially located as mlrB, mlrD, mlrA, and mlrC. The first MC-degrading enzyme MlrA (a 336-residue endopeptidase) encoded by mlrA gene in the degradative pathway can hydrolyze cyclic MC-LR at Adda-Arg bond into linearized MC-LR (Adda-Glu-Mdha-Ala-Leu-Masp-Arg-OH, MW = 1012) (Figure 1). Linearized MC-LR was then cleaved into a tetrapeptide (Adda-Glu-Mdha-Ala-OH, MW = 664) by the second enzyme MlrB encoded by mlrB gene at Ala-Leu bond. In the terminal step, the tetrapeptide was catalyzed further into some undetected smaller peptide fragments and amino acids by the third enzyme MlrC encoded by mlrC gene.
Theoretical aspects of peptide imprinting: screening of MIP (virtual) binding sites for their interactions with amino acids, di- and tripeptides
Published in Journal of the Chinese Advanced Materials Society, 2018
Julie Settipani, Kal Karim, Alienor Chauvin, Si Mohamed Ibnou-Ali, Florian Paille-Barrere, Evgeny Mirkes, Alexander Gorban, Lee Larcombe, Michael J. Whitcombe, Todd Cowen, Sergey A. Piletsky
The use of terminal sequences of target proteins as a surrogate template for the whole macromolecule was first proposed by Rachkov and Minoura in 2000. [1] They demonstrated that materials capable of binding the nonapeptide oxytocin, under aqueous conditions, could be prepared by imprinting a tetrapeptide with the same three amino acid residues in the N-terminus (Pro-Leu-Gly-NH2). The epitope approach was soon adapted by others to prepare materials capable of recognizing larger proteins, such as cytochrome c and even viruses. The concept of an ‘epitope’ has been borrowed from immunochemistry. In that context, it is the region of an antigen that is recognized by the variable domain of an antibody and could span adjacent residues on the antigen surface that are non-adjacent in the primary sequence. In imprinting terms however we normally mean an epitope to be a peptide with a single sequence (taken from the primary sequence of the target) that, when used as a template, generates a selective imprint for the said target. While many examples are terminal sequences, for some targets the protein termini may be inaccessible and a loop or other surface displayed region may be selected. A further advantage of using the epitope approach is that it is not necessary to isolate the target protein to use as template, provided that some structural information is known.