title: 4(R/S)-Amino/guanidino-substituted proline peptides: design, synthesis and DNA transfection properties.
abstract: Collagen is a major structural protein found in the connective tissues of higher organisms and mammals and its biomechanical properties are related to the high thermal stability of its triple helical structure. The primary structure of collagen is composed of the repeating tripeptide  motif of Pro-Hyp-Gly, where Hyp is 4 R -hydroxy proline. Cationic collagen mimetics consisting of [Pro(X)-Pro(Y)-Gly](6) where Pro(X) and Pro(Y) are 4(R/S)-amino/guanidine proline have been synthesized and shown to form triplexes more stable than the unmodified collagen  peptide [Pro-Hyp-Gly](6). The origin of hyperstability is due to conformational pre-organization of proline pucker arising from the electronegativity of the cationic group. These cationic collagen peptides are shown to be effective cell penetrating and plasmid DNA transfecting agents.  The results have potential for design of new collagen mimetics for biomaterial applications and efficient cell penetrating agents for drug delivery applications.
authors: Division of Organic Chemistry National Chemical laboratory, Pune, India.
authors: M
authors: M
authors: Umashankara
authors: Manaswini
authors: M
authors: Nanda
authors: Mahesh
authors: M
authors: Sonar
authors: Krishna N
authors: KN
authors: Ganesh
mesh_terms: D000588:Amines / Q000737:chemistry*; D004247:DNA / Q000737:chemistry*; D019791:Guanidine / Q000737:chemistry*; D008968:Molecular Conformation; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011392:Proline / Q000737:chemistry*; D013237:Stereoisomerism; D014162:Transfection
chemical_list: D000588:Amines; D010455:Peptides; D004247:DNA; D011392:Proline; D019791:Guanidine