Raquel Martin

Max Planck Institute for Intelligent Systems

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i-10 index

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Marie‐Madeleine Giraud‐Guille

Centre National de la Recherche Scientifique

David Hulmes

Université Claude Bernard Lyon 1

David L. Kaplan

Tufts University

J. Farjanel

Université Claude Bernard Lyon 1

Chad A. Mirkin

Northwestern University

Mark Cronin‐Golomb

Tufts University

D. Eichenberger

Bern University of Applied Sciences

Donna L. Wilson

Molecular Devices

Laurence Besseau

Biologie Intégrative des Organismes Marins

Sebastian Kruss

Ruhr University Bochum

Cooperative Institutions

Centre National de la Recherche Scientifique

Max Planck Institute for Intelligent Systems

Max Planck Society

Heidelberg University

Institut de Biologie et de Chimie des Protéines

Tufts University

Université Claude Bernard Lyon 1

Northwestern University

Sorbonne Université

Observatoire Océanologique de Banyuls-sur-Mer

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Surface Organization and Nanopatterning of Collagen by Dip Pen Nanolithography

Microscopy and Microanalysis (2002)

Donna L. Wilson Raquel Martin Mark Cronin‐Golomb Chad A. Mirkin David L. Kaplan

Journal Article Surface Organization and Nanopatterning of Collagen by Dip Pen Nanolithography Get access Donna L Wilson, Donna L Wilson Departments of Chemical and Biological Engineering and Bioengineering Center, Tufts University, Medford, MA 02155 Search for other works by this author on: Oxford Academic Google Scholar Raquel Martin, Raquel Martin Departments of Chemical and Biological Engineering and Bioengineering Center, Tufts University, Medford, MA 02155 Search for other works by this author on: Oxford Academic Google Scholar Mark Cronin-Golomb, Mark Cronin-Golomb Departments of Electrical Engineering and Computer Science and Bioengineering Center, Tufts University, Medford, MA 02155 Search for other works by this author on: Oxford Academic Google Scholar Chad A Mirkin, Chad A Mirkin Northwestern University, Department of Chemistry, Evanston, IL 60208-3113 Search for other works by this author on: Oxford Academic Google Scholar David L Kaplan David L Kaplan Departments of Chemical and Biological Engineering and Bioengineering Center, Tufts University, Medford, MA 02155 Search for other works by this author on: Oxford Academic Google Scholar Microscopy and Microanalysis, Volume 8, Issue S02, 1 August 2002, Pages 1020–1021, https://doi.org/10.1017/S1431927602102984 Published: 01 August 2002

Center (category theory)

10.1017/s1431927602102984

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Citations (5)

Liquid crystalline assemblies of collagen in bone and in vitro systems

Journal of Biomechanics (2003)

Marie‐Madeleine Giraud‐Guille Laurence Besseau Raquel Martin

Crimp

Procollagen peptidase

Polarized light microscopy

Collagen fibril

10.1016/s0021-9290(03)00134-9

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Citations (141)

Supramolecular assembly of collagen triblock peptides

Biopolymers (2003)

Raquel Martin Lars Waldmann David L. Kaplan

Abstract The relationship between primary sequence and collagen triple‐helix formation is relatively well characterized, while higher levels of structural assembly from these sequences is poorly understood. To address this gap, a new collagen‐like triblock peptide design was used to study the relationship between amino acid sequence and supramolecular assembly. Four collagen‐like peptides with the sequence (Glu) 5 (Gly–Xaa–Hyp–Gly–Pro–Hyp) 6 (Glu) 5 and corresponding to Xaa = alanine, proline, serine, or valine, and an analogous peptide without the glutamic acid end blocks, were solubilized in water at high concentrations (20–150 mg/mL) and analyzed in optical polarizing microscopy and transmission electron microscopy. Some of the peptides self‐assembled into supramolecular structures, the nature of which was determined by the core collagen‐like sequence. The globular end blocks appeared necessary for these short triple‐helix‐forming peptides to spontaneously organize into supramolecular structures in solution and also provided enhanced thermal stability based on CD analysis. The results indicate a strong dependence of the peptide triblock assembly behavior on the identity of the guest residue Xaa; nematic order when Xaa was valine, no organization when Xaa was serine, and banded spherulites displaying a cholesteric‐like twist when Xaa was proline or alanine. According to these results, the identity of the amino acid in position Xaa of the triplet Gly–Xaa–Yaa dramatically determined the type of supramolecular assembly formed by short triple helices based on collagen‐triblock like sequences. Moreover, the structural organization observed for these collagen‐triblock peptides was analogous to some assemblies observed for native collagen in vivo and in vitro. The amino acid sequence in the native collagen proteins may therefore be a direct determinant of the different supramolecular architectures found in connective tissues. © 2003 Wiley Periodicals, Inc. Biopolymers 70:435–444, 2003

Collagen helix

Alanine

Helix (gastropod)

Sequence (biology)

10.1002/bip.10464

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Citations (34)

Molecular liquid crystalline organisation of collagen in physiological conditions

Biology of the Cell (1999)

Raquel Martin David Hulmes J. Farjanel Marie‐Madeleine Giraud‐Guille

10.1016/s0248-4900(99)90114-4

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Citations (0)

Liquid crystalline ordering of procollagen as a determinant of three-dimensional extracellular matrix architecture 1 1Edited by M. F. Moody

Journal of Molecular Biology (2000)

Raquel Martin J. Farjanel D. Eichenberger Alain Colige Efrat Kessler

Procollagen peptidase

Crimp

Matrix (chemical analysis)

Polarized light microscopy

10.1006/jmbi.2000.3855

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Citations (67)

Surface organization and nanopatterning of collagen by dip-pen nanolithography

Proceedings of the National Academy of Sciences (2001)

Donna L. Wilson Raquel Martin Seunghun Hong Mark Cronin‐Golomb Chad A. Mirkin

Collagen is a key fibrous protein in biological systems, characterized by a complex structural hierarchy as well as the ability to self-assemble into liquid crystalline mesophases. The structural features of collagen influence cellular responses and material properties, with importance for a wide range of biomaterials and tissue architectures. The mechanism by which fibrillar collagen structures form from liquid crystalline mesophases is not well characterized. We report positive printing of collagen and a collagen-like peptide down to 30–50-nm line widths, using the atomic force microscopy technique of dip-pen nanolithography. The method preserved the triple-helical structure and biological activity of collagen and even fostered the formation of characteristic higher levels of structural organization. The “direct-write” capability of biologically relevant molecules, while preserving their structure and functionality, provides tremendous flexibility in future biological device applications and in proteomics arrays, as well as a new strategy to study the important hierarchical assembly processes of biological systems.

Dip-Pen Nanolithography

Biomolecule

10.1073/pnas.241323198

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Citations (292)

STABILITY OF DROSOPHILA CHROMOSOMES TO RADIOACTIVE DECAY OF INCORPORATED $sup 32$P

W.R. Lee Carol K Oden Carol A Bart Carole W Debney Raquel Martin

Radioactive decay

Source

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Stimulation of Cell Adhesion at Nanostructured Teflon Interfaces

Advanced Materials (2010)

Sebastian Kruss Tobias Wolfram Raquel Martin Stefanie Neubauer Horst Kessler

Tunable gold nanoparticle patterns have been immobilized onto amorphous teflon surfaces in a stable manner. This method provides a general route to covalently link biomolecules onto chemically inert teflon surfaces, which enhances endothelialization.

Inert

Biomolecule

Surface Modification

10.1002/adma.201003055

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Citations (42)

Large-Scale Production of Procollagen I from Chick Embryo Tendon Fibroblasts

Analytical Biochemistry (2000)

Raquel Martin J. Farjanel D. Eichenberger Marie‐Madeleine Giraud‐Guille David Hulmes

Procollagen peptidase

10.1006/abio.1999.4395

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