Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Amol S. Kotmale"'
Autor:
Prasad D. Dandekar, Amol S. Kotmale, Shrawan R. Chavan, Pranita P. Kadlag, Sangeeta V. Sawant, Dilip D. Dhavale, Ameeta RaviKumar
Publikováno v:
ACS Omega, Vol 6, Iss 3, Pp 1780-1786 (2021)
Externí odkaz:
https://doaj.org/article/4535c1f6b59248f09f91f673c750d4a5
Autor:
Sachin S. Burade, Sushil V. Pawar, Tanmoy Saha, Navanath Kumbhar, Amol S. Kotmale, Manzoor Ahmad, Pinaki Talukdar, Dilip D. Dhavale
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 15, Iss 1, Pp 2419-2427 (2019)
The intramolecular cyclization of a C-3-tetrasubstituted furanoid sugar amino acid-derived linear tetrapeptide afforded an oxazolone pseudo-peptide with the formation of an oxazole ring at the C-terminus. A conformational study of the oxazolone pseud
Externí odkaz:
https://doaj.org/article/b4e5b1688faf48808a050ce7a128e4f9
Autor:
Amol S. Kotmale, Dilip D. Dhavale, Sangeeta Sawant, Prasad D Dandekar, Pranita P Kadlag, Shrawan R. Chavan, Ameeta RaviKumar
Publikováno v:
ACS Omega, Vol 6, Iss 3, Pp 1780-1786 (2021)
ACS Omega
ACS Omega
Use of human pancreatic α-amylase (HPA) inhibitors is one of the effective antidiabetic strategies to lower postprandial hyperglycemia via reduction in the dietary starch hydrolysis rate. Many natural products from plants are being studied for their
Autor:
Amol S. Kotmale, Navnath M Kumbhar, Sachin S. Burade, Sushil V. Pawar, Dilip D. Dhavale, Pinaki Talukdar, Manzoor Ahmad, Tanmoy Saha
Publikováno v:
Beilstein Journal of Organic Chemistry
Beilstein Journal of Organic Chemistry, Vol 15, Iss 1, Pp 2419-2427 (2019)
Beilstein Journal of Organic Chemistry, Vol 15, Iss 1, Pp 2419-2427 (2019)
The C3-tetrasubstituted furanoid sugar amino acid derived linear amino acid dipeptide 8 and tetrapeptide 9 on intra-molecular cyclization afforded oxazolone pseudo-peptides 1 and 2a, respectively, with formation of oxazole ring at the C-terminus. Con
Autor:
Amol S. Kotmale, Rajesh G. Gonnade, Samir R. Shaikh, Tobias Stürzer, Rupesh L. Gawade, Deepak Kumar
Publikováno v:
Crystal Growth & Design. 19:5665-5678
A small library of ten sulfonamide derivatives comprising two aromatic rings was synthesized to investigate the effect of chronological positioning of the F-atom on the intramolecular π-stacking as...
Autor:
Amol S. Kotmale, Rajesh G. Gonnade, Krishnaprasad Madica, Krishna Chaitanya Nadimpally, Gangadhar J. Sanjayan
Publikováno v:
ChemistrySelect. 3:2776-2780
Autor:
Ekta Sangtani, Sachin S. Burade, Amol S. Kotmale, Dhiman Sarkar, Rajesh G. Gonnade, Gangadhar J. Sanjayan, Pattuparambil R. Rajamohanan
Publikováno v:
New Journal of Chemistry. 42:1197-1201
This paper reports conformational changes observed in cyclic bioactive peptides such as gramicidin S and avellanin upon incorporation of a pseudo-β (C9) Ant–DPro turn motif in their structural frameworks. Solution-state studies suggested that a sy
Autor:
Naresh Bhuma, Navanath Kumbhar, Tanmoy Saha, Rajesh G. Gonnade, Sachin S. Burade, Amol S. Kotmale, Pinaki Talukdar, Pattuparambil R. Rajamohanan, Dilip D. Dhavale
Publikováno v:
Organic Letters. 19:5948-5951
Syntheses of fluorinated sugar amino acid derived α,γ-cyclic tetra- and hexapeptides are reported. The IR, NMR, ESI-MS, CD, and molecular modeling studies of cyclic tetra- and hexapeptides showed C2 and C3 symmetric flat oval- and triangular-ring s
Autor:
Rajesh G. Gonnade, Sachin B. Baravkar, Samir R. Shaikh, Gangadhar J. Sanjayan, Amol S. Kotmale
Publikováno v:
European Journal of Organic Chemistry. 2017:2944-2949
In 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
Autor:
Sopan Valiba Shinde, Dilip D. Dhavale, Amol S. Kotmale, Sachin S. Burade, Rajesh G. Gonnade, Naresh Bhuma, Pattuparambil R. Rajamohanan, Pinaki Talukdar, Navanath Kumbhar
Publikováno v:
The Journal of Organic Chemistry. 82:5826-5834
Acyclic αγα-tripeptides derived from fluorinated-furanoid sugar amino acid frameworks act as reverse-turn inducers with a U-shaped conformation, whereas the corresponding nonfluorinated αγα-tripeptides show random peptide conformations. The NMR