<?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%">Santhiya, Deenan</style></author><author><style face="normal" font="default" size="100%">Dias, Rita S.</style></author><author><style face="normal" font="default" size="100%">Dutta, Sounak</style></author><author><style face="normal" font="default" size="100%">Das, Prasanta Kumar</style></author><author><style face="normal" font="default" size="100%">Miguel, Maria G.</style></author><author><style face="normal" font="default" size="100%">Lindman, Bjorn</style></author><author><style face="normal" font="default" size="100%">Maiti, Souvik</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Kinetic studies of amino acid-based surfactant binding to DNA</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Physical Chemistry B</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2012</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%">20</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%">116</style></volume><pages><style face="normal" font="default" size="100%">5831-5837</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In this work, the binding kinetics of amino acid-based surfactants, presenting different linkers and head groups, with calf thymus (CT)-DNA was studied using stopped-flow fluorescence spectroscopy. The kinetic studies were carried out as a function of Na+ concentration and surfactant-to-DNA charge ratio. The surfactant binding on DNA took place in two consecutive steps, for which the corresponding first and second relative rate constants (k(1) and k(2)) were determined. The fast step was attributed to the surfactant binding to DNA and micelle formation in its vicinity, the slower step to DNA condensation and possible rearrangement of the surfactant aggregates. In general, both relative rate constants increase with surfactant concentration and decrease with the ionic strength of the medium. The architecture of the surfactant was found to have a significant impact on the kinetics of the DNA surfactant complexation. Surfactants with amide linkers showed larger relative rate constants than those with ester linkers. The variation of the relative rate constants with the head groups of the surfactants, alanine and proline, was found to be less obvious, being partially dependent on the surfactant concentration.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.607
</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></records></xml>