@article {2456,
	title = {Nanomechanical Properties of Tenascin-X Revealed by Single-Molecule Force Spectroscopy},
	journal = {Journal of Molecular Biology},
	volume = {385},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 403HJTimes Cited: 4Cited Reference Count: 35Jollymore, Ashlee Lethias, Claire Peng, Qing Cao, Yi Li, Hongbin},
	month = {Jan},
	pages = {1277-1286},
	type = {Article},
	abstract = {Tenascin-X is an extracellular matrix protein and binds a variety of molecules in extracellular matrix and on cell membrane. Tenascin-X plays important roles in regulating the structure and mechanical properties of connective tissues. Using single-molecule atomic force microscopy, we have investigated the mechanical properties of bovine tenascin-X in detail. Our results indicated that tenascin-X is an elastic protein and the fibronectin type III (FnIII) domains can unfold under a stretching force and refold to regain their mechanical stability upon the removal of the stretching force. All the 30 FnIII domains of tenascin-X show similar mechanical stability, mechanical unfolding kinetics, and contour length increment upon domain unfolding, despite their large sequence diversity. In contrast to the homogeneity in their mechanical unfolding behaviors, FnIII domains fold at different rates. Using the 10th FnIII domain of tenascin-X (TNXfn10) as a model system, we constructed a polyprotein chimera composed of alternating TNXfn10 and GB1 domains and used. atomic force microscopy to confirm that the mechanical properties of TNXfn10 are consistent with those of the FnIII domains of tenascin-X These results lay the foundation to further study the mechanical properties of individual FnIII domains and establish the relationship between point mutations and mechanical phenotypic effect on tenascin-X Moreover, our results provided the opportunity to compare the mechanical properties and design of different forms of tenascins. The comparison between tenascin-X and tenascin-C revealed interesting common as well as distinguishing features for mechanical unfolding and folding of tenascin-C and tenascin-X and will open up new avenues to investigate the mechanical. functions and architectural design of different forms of tenascins. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {AFM, BINDING, DEFICIENCY, DOMAINS, FAMILY, FnIII domains, IDENTIFICATION, III MODULES, MECHANICAL STABILITY, mechanical unfolding, microscopy, PROTEIN, single molecule force spectroscopy, tenascin},
	isbn = {0022-2836},
	url = {<Go to ISI>://000263073400022},
	author = {Jollymore, A. and Lethias, C. and Peng, Q. and Cao, Y. and Li, H. B.}
}
@article {1428,
	title = {Blood compatibility of novel water soluble hyperbranched polyglycerol-based multivalent cationic polymers and their interaction with DNA},
	journal = {Biomaterials},
	volume = {27},
	number = {31},
	year = {2006},
	note = {ISI Document Delivery No.: 085NOTimes Cited: 48Cited Reference Count: 41Kainthan, Rajesh Kumar Gnanamani, Muthiah Ganguli, Munia Ghosh, Tanay Brooks, Donald E. Maiti, Souvik Kizhakkedathu, Jayachandran N.},
	month = {Nov},
	pages = {5377-5390},
	type = {Article},
	abstract = {A novel class of hyperbranched polymers based on polyglycerol (PG) and poly(ethylene glycol) (PEG) are synthesized by multibranching anionic ring opening polymerization. Multivalent cationic sites are added to these polymers by a post-amination and quarternization reactions. Blood compatibility studies using these polymers at different concentrations showed insignificant effects on complement activation, platelet activation, coagulation, erythrocyte aggregation and hemolysis compared to branched cationic polyethyleneimine (PEI). The degree of quarternization does not have large influence on the blood compatibility of the new polymers. Cytotoxicity of these polymers is significantly lower than that of PEI and is a function of quarternized nitrogen present in the polymer. Also, these polymers bind DNA in the nanomolar range and are able to condense DNA to highly compact, stable, water soluble nanoparticles in the range of 60-80 nm. Gel electrophoresis studies showed that they form electroneutral complexes with DNA around N/P ratio 1 irrespective of the percentage of quarternization under the conditions studied. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {AFM, blood-compatibility, cationic polymers, COAGULATION, COMPLEXES, delivery, DNA, drug, GENE DELIVERY, hyperbranched polymers, IN-VITRO, MOLECULAR-WEIGHT, NANOPARTICLES, OPPOSITELY CHARGED SURFACTANT, PLATELETS, RANDOM COPOLYMER, therapy},
	isbn = {0142-9612},
	url = {<Go to ISI>://000240611000005},
	author = {Kainthan, R. K. and Gnanamani, M. and Ganguli, M. and Ghosh, T. and Brooks, D. E. and Maiti, S. and Kizhakkedathu, J. N.}
}
@article {1555,
	title = {Engineering proteins with novel mechanical properties by recombination of protein fragments},
	journal = {Angewandte Chemie-International Edition},
	volume = {45},
	number = {34},
	year = {2006},
	note = {ISI Document Delivery No.: 082MRTimes Cited: 20Cited Reference Count: 51Sharma, Deepak Cao, Yi Li, Hongbin},
	pages = {5633-5638},
	type = {Article},
	keywords = {AFM, ATOMIC-FORCE MICROSCOPY, ELASTICITY, EVOLUTION, IG DOMAIN, IMMUNOGLOBULIN DOMAINS, MOLECULAR-DYNAMICS SIMULATIONS, protein engineering, protein structures, scanning probe microscopy, SINGLE PROTEIN, single-molecule studies, SPECTROSCOPY, STABILITY, TITIN},
	isbn = {1433-7851},
	url = {<Go to ISI>://000240391400016},
	author = {Sharma, D. and Cao, Y. and Li, H. B.}
}
@article {866,
	title = {Molecular weight and polydispersity estimation of adsorbing polymer brushes by atomic force microscopy},
	journal = {Langmuir},
	volume = {20},
	number = {8},
	year = {2004},
	note = {ISI Document Delivery No.: 811CPTimes Cited: 23Cited Reference Count: 36},
	month = {Apr},
	pages = {3297-3303},
	type = {Article},
	abstract = {{We have estimated the molecular weight, M-n, and polydispersity, PDI, of densely grafted poly(N-isopropylacrylamide) (PNIPAM) brushes using a novel atomic force microscopy (AFM) approach. When compression of a polymer brush induced adsorption of multiple chains to an AFM tip, the resulting decompression force profile exhibited a maximum attractive force at a separation, L-m, that decayed to zero with increasing tip-sample separation. We have found that the separation L approximates the average contour length, L,, determined by gel permeation chromatography (GPC). The detection of a decaying attractive force at separations larger than L, suggests that chains of above average length sequentially break free from the tip as they are stretched away from the grafting surface. The shape of the decompression profile in this region approximately paralleled the cumulative weight fraction of the grafted chains determined by GPC. The fraction of chains of a given molecular weight determined from a single force curve fit a log-normal distribution, having a standard deviation that provided an estimate of the PDL We have characterized two PNIPAM brushes by this AFM technique as well as by GPC coupled to a multiangle laser light-scattering detector (MALLS). The values obtained by AFM-(1) Mn,(AFM) = (3.8 +/- 0.5) X 104},
	keywords = {ADSORPTION, AFM, CHAIN ELONGATION, ELASTIC PROPERTIES, PHASE, POLY(ACRYLAMIDE), POLY(N-ISOPROPYLACRYLAMIDE), SPECTROSCOPY, SURFACES},
	isbn = {0743-7463},
	url = {<Go to ISI>://000220750300044},
	author = {Goodman, D. and Kizhakkedathu, J. N. and Brooks, D. E.}
}
