Публикации - Пептиды

Self-assembly of short peptides composed of only aliphatic amino acids and a combination of aromatic and aliphatic amino acids
Chilukuri Subbalakshmi, Sunkara V. Manorama, Ramakrishnan Nagaraj
Journal of Peptide Science, 2012, ISSN: 1099-1387, Том: 18, Выпуск: 5, Стр.: 283-292, DOI: 10.1002/psc.2395

Novel dipeptide nanoparticles for effective curcumin delivery
Shadab Alam, Jiban J. Panda, Virander S. Chauhan
International journal of nanomedicine, 2012, Том: 7, Стр.: 4207, DOI: 10.2147/IJN.S33015

Probing the role of aromaticity in the design of dipeptide based nanostructures
Aseem Mishra, Virander Singh Chauhan
Nanoscale, 2011, ISSN: 2040-3372, Том: 3, Выпуск: 3, Стр.: 945-949, DOI: 10.1039/C0NR00691B

Designed peptides as model self-assembling nanosystems: characterization and potential biomedical applications
Jiban J Panda, Ankur Kaul, Shadab Alam, Anil K Babbar, Anil K Mishra, Virander S Chauhan
Therapeutic Delivery, 2011, ISSN: 2041-5990, Том: 2, Выпуск: 2, Стр.: 193-204, DOI: 10.4155/tde.10.93

Clickable Functionalization of Liposomes with the gH625 Peptide from Herpes simplex Virus Type I for Intracellular Drug Delivery
Rossella Tarallo, Antonella Accardo, Annarita Falanga, Daniela Guarnieri, Giuseppe Vitiello, Paolo Netti, Gerardino D'Errico, Giancarlo Morelli, Stefania Galdiero
Chemistry – A European Journal, 2011, ISSN: 1521-3765, Том: 17, Выпуск: 45, Стр.: 12659-12668, DOI: 10.1002/chem.201101425

Impact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils
Nitin Chaudhary, Ramakrishnan Nagaraj
Journal of Peptide Science, 2011, ISSN: 1099-1387, Том: 17, Выпуск: 2, Стр.: 115-123, DOI: 10.1002/psc.1339

Acceleration of protein aggregation by amphiphilic peptides: Transformation of supramolecular structure of the aggregates
N. V. Artemova, V. A. Stein-Margolina, Z. M. Bumagina, B. Ya. Gurvits
Biotechnology Progress, 2011, ISSN: 1520-6033, Том: 27, Выпуск: 3, Стр.: 846-854, DOI: 10.1002/btpr.574

Peptide modified nanocarriers for selective targeting of bombesin receptors
Antonella Accardo, Rosalba Mansi, Anna Morisco, Gaetano Mangiapia, Luigi Paduano, Diego Tesauro, Aurel Radulescu, Michela Aurilio, Luigi Aloj, Claudio Arra
Molecular BioSystems, 2010, ISSN: 1742-2051, Том: 6, Выпуск: 5, Стр.: 878-887, DOI: 10.1039/B923147A

Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins
N. V. Artemova, Z. M. Bumagina, A. S. Kasakov, V. V. Shubin, B. Ya. Gurvits
Peptides, 2010, ISSN: 0196-9781, Том: 31, Выпуск: 2, Стр.: 332-338, DOI: 10.1016/j.peptides.2009.11.025

Amphotericin B interactions with soluble oligomers of amyloid Aβ1-42 peptide
Nicholas W. Smith, Onofrio Annunziata, Sergei V. Dzyuba
Bioorganic & Medicinal Chemistry, 2009, ISSN: 0968-0896, Том: 17, Выпуск: 6, Стр.: 2366-2370, DOI: 10.1016/j.bmc.2009.02.016