<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Patil, Kiran M.</style></author><author><style face="normal" font="default" size="100%">Naik, Rangeetha J.</style></author><author><style face="normal" font="default" size="100%">Vij, Manika</style></author><author><style face="normal" font="default" size="100%">Yadav, Amit K.</style></author><author><style face="normal" font="default" size="100%">Kumar, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Ganguli, Munia</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Second generation, arginine-rich (R-X `-R)(4)-type cell-penetrating alpha-omega-alpha-peptides with constrained, chiral omega-amino acids (X `) for enhanced cargo delivery into cells</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">(R-X-R)-motif</style></keyword><keyword><style  face="normal" font="default" size="100%">alpha-omega-alpha-Peptide</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell-penetrating peptide</style></keyword><keyword><style  face="normal" font="default" size="100%">Constrained chiral amino acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptidomimetics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">17</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">4198-4202</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The syntheses of novel N-aminoalkyl proline-derived spacers (X') in polycationic (R-X'-R)-motif cell-penetrating alpha-omega-alpha-peptides are described as improved molecular transporters and their structural features studied by CD. FACS analysis shows enhanced cellular uptake and confocal microscopy indicates predominantly cytoplasmic localization. The oligomers are efficient at transporting pDNA into cells. The chirality together with the hydrophobicity and flexibility derived from the spacer chain are found to have marked influence on the cell-penetrating and cargo delivery properties of the cell-penetrating peptides (CPPs). The peptides containing N-(3-aminopropyl)-D-proline spacers are found to be the best at cell penetration and cargo delivery in the present study. (C) 2014 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">17</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.19</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Natarajan, Poornemaa</style></author><author><style face="normal" font="default" size="100%">Patil, Kiran M.</style></author><author><style face="normal" font="default" size="100%">Vij, Manika</style></author><author><style face="normal" font="default" size="100%">Yadav, Amit K.</style></author><author><style face="normal" font="default" size="100%">Kumar, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Ganguli, Munia</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">RXR-carbamate - a novel molecular transporter for skin</style></title><secondary-title><style face="normal" font="default" size="100%">Molecular Therapy</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">Amer Soc Gene &amp; Cell Therapy</style></publisher><pub-location><style face="normal" font="default" size="100%">75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA</style></pub-location><volume><style face="normal" font="default" size="100%">23</style></volume><pages><style face="normal" font="default" size="100%">S64-S64</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><notes><style face="normal" font="default" size="100%">18th Annual Meeting of the American-Society-of-Gene-and-Cell-Therapy (ASGCT), New Orleans, LA, MAY 13-16, 2015</style></notes><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">6.938</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Vij, Manika</style></author><author><style face="normal" font="default" size="100%">Natarajan, Poornemaa</style></author><author><style face="normal" font="default" size="100%">Yadav, Amit K.</style></author><author><style face="normal" font="default" size="100%">Patil, Kiran M.</style></author><author><style face="normal" font="default" size="100%">Pandey, Tanuja</style></author><author><style face="normal" font="default" size="100%">Gupta, Nidhi</style></author><author><style face="normal" font="default" size="100%">Santhiya, Deenan</style></author><author><style face="normal" font="default" size="100%">Kumar, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author><author><style face="normal" font="default" size="100%">Ganguli, Munia</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Efficient cellular entry of (r-x-r)-type carbamate-plasmid DNA complexes and its implication for noninvasive topical DNA delivery to skin</style></title><secondary-title><style face="normal" font="default" size="100%">Molecular Pharmaceutics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cell penetrating peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">nucleic acid delivery</style></keyword><keyword><style  face="normal" font="default" size="100%">skin penetration</style></keyword><keyword><style  face="normal" font="default" size="100%">transfection</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">6</style></number><publisher><style face="normal" font="default" size="100%">AMER CHEMICAL SOC</style></publisher><pub-location><style face="normal" font="default" size="100%">1155 16TH ST, NW, WASHINGTON, DC 20036 USA</style></pub-location><volume><style face="normal" font="default" size="100%">13</style></volume><pages><style face="normal" font="default" size="100%">1779-1790</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Arginine-rich cell penetrating peptides are powerful tools for in vitro as well as in vivo delivery of a wide plethora of biomolecules. However, presence of consecutive arginine residues leads to enhanced amenability for proteolytic degradation as well as steric hindrances for membrane interactions which compromise its bioavailability. In order to overcome these limitations we previously reported a safe and stable octaarginine based oligomer, i.e., (r-x-r)4-carbamate, where the backbone amide linkages were replaced by carbamate linkages and 6-aminohexanoic acid based spacer moieties were incorporated for better flexibility, hydrophobicity, optimal spacing of guanidinium groups, and protection against proteolytic cleavage; resulting in improved transfection efficiency over its amide counterpart. In the present work we have investigated the mechanism behind this enhanced transfection efficiency and, based on our observations, demonstrate how the synergistic effect of rationalized oligomer designing, complex characteristics, and cell type contributes to overall effective intracellular delivery. Our results indicate that the (r-x-r)4-carbamate plasmid DNA complexes primarily utilize lipid raft dependent pathway of cellular entry more than other pathways, and this possibly facilitates their increased entry in the lipid raft rich milieu of skin cells. We also emphasize the utility of oligomer (r-x-r)4-carbamate as an efficient carrier for topical delivery of nucleic acids in skin tissue. This carrier can be utilized for safe, efficient, and noninvasive delivery of therapeutically relevant macromolecular hydrophilic cargo like nucleic acids to skin.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">4.342</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sailthedkar, Nidhi S.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Yadav, Amit K.</style></author><author><style face="normal" font="default" size="100%">Seal, Shubhendu</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Phyto-inspired cyclic peptides derived from plant Pin-II type protease inhibitor reactive center loops for crop protection from insect pests</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimica ET Biophysica Acta-General Subjects</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cyclic peptide</style></keyword><keyword><style  face="normal" font="default" size="100%">Lepidoptera</style></keyword><keyword><style  face="normal" font="default" size="100%">Pest control</style></keyword><keyword><style  face="normal" font="default" size="100%">protease inhibitor</style></keyword><keyword><style  face="normal" font="default" size="100%">Reactive loop</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1863</style></volume><pages><style face="normal" font="default" size="100%">1254-1262</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Background: Natural defence of plants against insect pests involves protease inhibitors (PIs) that interfere with insect digestive proteases. Pin-II type plant PIs are wound inducible upon insect damage and possess multiple inhibitory repeat domains that can inhibit trypsin and chymotrypsin-like proteases in the insect midgut. Yet, their agricultural ex-vivo application is limited due to large molecular size and environmental instability, which could be overcome by small peptides. Methods: Bicyclic peptides were designed by grafting Pin-II PIs derived reactive center loop (RCL) on synthetic tris(bromomethyl)benzene scaffold. In vitro binding with trypsin-like proteases was evaluated by biochemical and biophysical assays, followed by molecular dynamics simulations. In vivo effects on two major lepidopteran insect pests, Helicoverpa armigera and Spodoptera litura were studied upon feeding with peptide treated leaves. Affinity based pull down assays were used to identify target proteins in insect gut. Results: Bicyclic RCLs showed ten-fold enhanced protease inhibition compared to their linear counterparts. They exhibited feeding deterrence and growth reduction of lepidopteran insects. Bicyclic peptides predominantly interact with midgut serine proteases. Possible binding modes involve simultaneous interaction with the active site and specificity-determining residues of insect gut trypsin. Conclusion: Bicyclic peptides are potent inhibitors of serine proteases in the insect midgut. They cause feeding aversion and larval growth retardation. Bi-domain cyclic peptides interact with two sites on trypsin, leading to enhanced efficacy over linear RCL peptides. General significance: Bicyclic peptides mimic natural PIs by inhibiting insect proteases leading to growth reduction, thus, could be used as pest control molecules in agriculture.&lt;/p&gt;
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