Biological Properties of Poly-a-Amino

Sela, M., and Katchalski, E., Biological properties of poly-a-amino acids, Adv. Prot. Chem.. 14. 391-479, 1959. 

The kinetics and mechanism of polymerization of IV-carboxy-a-amino acid anhydrides as well as the biological properties of poly-a-amino acids have been studied and reviewed extensively (70,79,80). The critical chain length for helix formation varies from one amino acid to another (81,82). The critical chain length in L-methionine oligopeptides is the heptamer (83). 

Pseudo-poly(amino acids) were first described in 1984 (Kohn, 1984) and have since been evaluated for use in several medical applications (Kohn, 1987 Yu-Kwon, 1989 Zhou, 1990 Kohn, 1993 Mao, 1993). Although a range of different pseudo-poly(amino acids) has been prepared, detailed studies of the physical properties, biological properties, and possible applications of these polymers have so far been conducted only for a select group of new tyrosine- derived polycarbonates, polyiminocarbonates, and polyarylates. This review will encompass the work to date on these specific materials. 

Song H, Chu C. Synthesis and characterization of a new family of cationic amino acid-based poly(ester amide)s and their biological properties. J Appl Polym Sci 2012 124(5) 3840-53. 

The cell distribution of 3-amino-4-hydroxymethyl acridine derivatives 70 (Scheme 25), which has the N3—C4—16 substitution pattern, was studied by real-time fluorescence microscopy and SIMS structured illumination microscopy). The latter method required the introduction of an iodine atom at position 6 of the acridine which influences the Upophihcity but does not modify significantly the biological properties such as IC50 and subcellular localization (2009EJMC4758). A co-polymer 71 consisting of water-soluble maleic anhydride-containing poly[maleic anhydride-u/i-acrylic acid] (poly(MA-alt-AA) or MAAA) copolymer was modified with acriflavine (AF) which displayed antibacterial activity on EHEC and Staphylococcus aureus (2014MI2903). 

Elastin-like polypeptides (ELPs) have been extensively studied due to the fact that they combine similar stimulus response properties to other artificial polymers such as poly(A-isopropylacrylamide) (pNIPAM) with the advantages of a biologically derived material, that is, it is biocompatible, modular in its composition, and can be obtained by biological processes. ELPs are polypeptides that contain a short, repetitive peptide sequence, most commonly (VPGXG) that is derived from tropoelastin, the precursor of elastin. In this sequence, X represents any amino acid sequence except proUne. Polypeptides composed of the pentapeptide repeat unit VPGXG possess a reversible lower critical solution temperature (LCST). Below the LCST, the peptide is soluble... 

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