01539nas a2200181   4500008004100000022001400041245006500055210006300120260011000183300001600293490000700309520084400316100002101160700002501181700002401206700002801230856009901258       2014                        eng d  a1359-734500aSynthetic turn mimetics and hairpin nucleators: quo vadimus?0 aSynthetic turn mimetics and hairpin nucleators quo vadimus  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcOCT  a13874-138840 v503 a<p>Structural mimicry of peptides has witnessed perceptible progress in the last three decades. Reverse turn and beta-hairpin units are the smallest secondary structural motifs that are some of the most scrutinized functional cores of peptides and proteins. The practice of mimicking, without altering the function of the bioactive core, ranges from conformational locking of the basic skeleton to total replacement of structural architecture using synthetic analogues. Development of heterogeneous backbones - using unnatural residues in place of natural ones - has broadened further opportunities for efficient structural rigidification. This feature article endeavours to trail the path of progress achieved hitherto and envisage the possibilities that lie ahead in the development of synthetic turn mimetics and hairpin nucleators.</p>1 aNair, Roshna, V.1 aBaravkar, Sachin, B.1 aIngole, Tukaram, S.1 aSanjayan, Gangadhar, J.  uhttp://library.ncl.res.in/content/synthetic-turn-mimetics-and-hairpin-nucleators-quo-vadimus-001255nas a2200169   4500008004100000245010300041210006900144260000800213300001600221520059600237100002500833700002200858700002100880700003100901700002800932856012500960       2017                        eng d00aStructural insights into the hydrogen-bonding and folding pattern in ant-ant-pro-gly tetrapeptides0 aStructural insights into the hydrogenbonding and folding pattern  cMAY  a2944–29493 aIn this paper, we provide structural insights into the hydrogen-bonding and folding pattern in Ant-Ant-Pro-Gly tetrapeptides (Ant: anthranilic acid; Pro: proline; and Gly: glycine). Comparison of the C-terminal esters and their amide analogs revealed strikingly different H-bonding networks. Whereas the ester analogs displayed an open structure without terminal H-bonding interactions, the amide analogs showed a completely folded structure. Structural details were revealed by using a combination of X-ray crystal structure studies and NOE-based molecular dynamics (MD) simulation studies.1 aBaravkar, Sachin, B.1 aKotmale, Amol, S.1 aMobin, Samir, R.1 aGonnade, Rajesh, Ghanshyam1 aSanjayan, Gangadhar, J.  uhttp://library.ncl.res.in/content/structural-insights-hydrogen-bonding-and-folding-pattern-ant-ant-pro-gly-tetrapeptides01418nas a2200181   4500008004100000245011300041210006900154260000800223300001400231490000700245520074500252100002500997700002301022700001901045700001801064700002801082856012601110       2018                        eng d00aSynthesis and anticancer activity of conformationally constrained Smac mimetics containing pseudo beta turns0 aSynthesis and anticancer activity of conformationally constraine  cSEP  a3473-34760 v593 aHerein, we report synthesis and in vitro anticancer activity of conformationally constrained Smac mimetics containing reverse turn inducing motifs "Ant-Pro" and "sAnt-Pro". The synthesis of Smac analogs with diverse hydrophobic groups at the C-terminus was carried out using solution phase peptide synthesis. The synthesis of Ant-Pro containing analogs 3a-j was carried out by ring opening of benzoxazinones 7a-c, whereas, their sulfonamide counterparts 4a-h were synthesized by using routine acid-amine coupling reaction. In vitro anticancer studies against breast cancer cell line MDA-MB-231 revealed that some of the new analogs had better anticancer activity than the standard AVPI Smac tetrapeptide. (C) 2018 Published by Elsevier Ltd.1 aBaravkar, Sachin, B.1 aWagh, Mahendra, A.1 aPaul, Debasish1 aSantra, Manas1 aSanjayan, Gangadhar, J.  uhttp://library.ncl.res.in/content/synthesis-and-anticancer-activity-conformationally-constrained-smac-mimetics-containing