4(R/S)-Amino/Guanidino-substituted Proline Peptides: Design, Synthesis and DNA Transfection Properties

Authors

  • M. Umashankara Division of Organic Chemistry National Chemical laboratory Pune 411008, India
  • Manaswini Nanda Division of Organic Chemistry National Chemical laboratory Pune 411008, India
  • Mahesh Sonar Division of Organic Chemistry National Chemical laboratory Pune 411008, India
  • Krishna N. Ganesh Indian Institute of Science Education and Research Pune 411008, India; Division of Organic Chemistry National Chemical laboratory Pune 411008, India. kn.ganesh@iiserpune.ac.in

DOI:

https://doi.org/10.2533/chimia.2012.936

Keywords:

4-aminoproline peptides, Cationic collagen mimetics, Cell penetrating peptides, 4-guanidino proline peptides

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.

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Published

2012-12-19

Issue

Section

Scientific Articles

How to Cite

[1]
M. Umashankara, M. Nanda, M. Sonar, K. N. Ganesh, Chimia 2012, 66, 936, DOI: 10.2533/chimia.2012.936.