02114nas a2200241   4500008004100000022001400041245008000055210006900135260011000204300001400314490000700328520119600335100003301531700002101564700002301585700002201608700002601630700002401656700002601680700003501706700002801741856010301769       2013                        eng d  a1477-052000aEster vs. amide on folding: a case study with a 2-residue synthetic peptide0 aEster vs amide on folding a case study with a 2residue synthetic  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcDEC  a8348-83560 v113 a<p>Although known for their inferiority as hydrogen-bonding acceptors when compared to amides, esters are often found at the C-terminus of peptides and synthetic oligomers (foldamers), presumably due to the synthetic readiness with which they are obtained using protected peptide coupling, deploying amino acid esters at the C-terminus. When the H-bonding interactions deviate from regularity at the termini, peptide chains tend to ``fray apart''. However, the individual contributions of C-terminal esters in causing peptide chain end-fraying goes often unnoticed, particularly due to diverse competing effects emanating from large peptide chains. Herein, we describe a striking case of a comparison of the individual contributions of C-terminal ester vs. amide carbonyl as a H-bonding acceptor in the folding of a peptide. A simple two-residue peptide fold has been used as a testing case to demonstrate that amide carbonyl is far superior to ester carbonyl in promoting peptide folding, alienating end-fraying. This finding would have a bearing on the fundamental understanding of the individual contributions of stabilizing/destabilizing non-covalent interactions in peptide folding.</p>1 aVijayadas, Kuruppanthara, N.1 aNair, Roshna, V.1 aGawade, Rupesh, L.1 aKotmale, Amol, S.1 aPrabhakaran, Panchami1 aGonnade, Rajesh, G.1 aPuranik, Vedavati, G.1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/ester-vs-amide-folding-case-study-2-residue-synthetic-peptide-0