Role of Aspartic Acid in Collagen Structure and Stability:  A Molecular Dynamics Investigation

Raman, Srivatsan; Parthasarathi, Ramakrishnan; Subramanian, V.; Ramasami, T.

doi:10.1021/jp0625715

Cited by 28 publications

(27 citation statements)

References 59 publications

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“…8D). The increased flexibility of amino acid-rich triple helices compared with imino acid-rich triple helices is in line with previous MD analyses of other collagen-like polypeptides (47)(48)(49).…”

Section: Scl23-v Structurally Resembles Gp41-supporting

confidence: 89%

The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41

Squeglia

Bachert

Simone

et al. 2014

Journal of Biological Chemistry

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Background: Streptococcal collagen-like proteins play crucial roles in host adhesion, host cell entry, and immunomodulation of host defenses. Results: This study provides the first three-dimensional structural description of a streptococcal collagen-like protein. Conclusion:The crystal structure evidences a six-helical bundle fold, which is unusual in bacterial proteins and characteristic of viral fusion proteins. Significance: The high resolution structure provides a structural basis for the design of inhibitors of streptococcal invasion.

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Section: Scl23-v Structurally Resembles Gp41-supporting

confidence: 89%

The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41

Squeglia

Bachert

Simone

et al. 2014

Journal of Biological Chemistry

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“…The differential stability of CP with Asp in the X AA and Y AA positions has been attributed to the changes in the flexibility of the backbone and solvation. 44 The presence of ion pairs in the collagen-like sequence has also been analyzed with the help of MD simulation. 45 Despite the wealth of literature on the sequence-dependent stability of model CPs, studies on the inter-relationship between the sequence length and molecular stability have been limited.…”

Section: Introductionmentioning

confidence: 99%

Role of Length-Dependent Stability of Collagen-like Peptides

et al. 2008

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Understanding the structure, folding, and stability of collagen is complex because of its length and variations in the amino acid (AA) sequence composition. It is well known that the basic constituent of the collagen helix is the triplet repeating sequence of the form Gly-X(AA)-Y(AA). On the basis of previous models and with the frequency of occurrence of the triplets, the ((Gly-Pro-Hyp)n)3 (where n is the number of triplets) sequence replicate has been chosen as the model for the most stable form of the collagen-like sequence. With a view to understand the role of sequence length (or the number of triplets) on the stability of collagen, molecular dynamics simulations have been carried out by varying the number of triplet units on the model collagen-like peptides. The results reveal that five triplets are required to form the stable triple helix. Further analysis shows that the intermolecular structural rigidity of the imino acid residues, hydrogen bonding, and water structure around the three chains of the triple helix play the dominant roles on its structure, folding, and stabilization.

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“…Proton signal was observed with a relatively low spinning rate of 2.6 kHz to reduce the phase-separation effects of the centrifugal force caused by sample spinning. The NMR spectrum was recorded using a small angle excitation (30 ) and a recovery time 10 s.…”

Section: Hr-mas Nmr Analysismentioning

confidence: 99%

Stimuli responsive deswelling of radiation synthesized collagen hydrogel in simulated physiological environment

Zhang

Wei

et al. 2012

J Biomedical Materials Res

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Collagen hydrogels were prepared via radiation crosslinking. The simulated physiological environmental effects related to their biomedical applications on the volume phase transition of collagen hydrogel were studied, that is stimuli response to ions, temperature, and pH. The deswelling behavior of collagen hydrogel depends on the salt concentration, temperature, pH, and the hydrogel preparation procedure. Meanwhile, hydrogel structure related to the volume phase transition was investigated by FTIR, fluorescence spectrum, and HR-MAS NMR. Deswelling in salt solution caused little change on collagen conformation, and a denser network led to more significant tyrosine-derived fluorescence quenching. Hydrogen bonding between hydrated water and collagen polypeptide chain was dissociated and the activity of hydrophobic side chain increased, inducing a higher extent of contraction with the increasing of salt concentration. Moreover, salt solution treatments weakened the electrostatic interactions, side chains interactions, and hydrogen bonding of collagen hydrogel, which reduced the thermal stability of collagen hydrogel. Comparing with cell-free collagen hydrogel contraction, fibroblasts did not aggravate contraction of collagen hydrogel significantly. This study elucidated the deswelling mechanism of radiation crosslinked collagen hydrogel in simulated physiological environment and provides strategies for controlling the stimuli response of collagen hydrogel in biomedical application.

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Role of Aspartic Acid in Collagen Structure and Stability: A Molecular Dynamics Investigation

Cited by 28 publications

References 59 publications

The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41

The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41

Role of Length-Dependent Stability of Collagen-like Peptides

Stimuli responsive deswelling of radiation synthesized collagen hydrogel in simulated physiological environment

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