Hydration structure of a collagen peptide

Bella, Jordi; Brodsky, Barbara; Berman, Helen M.

doi:10.1016/s0969-2126(01)00224-6

Cited by 582 publications

(613 citation statements)

References 41 publications

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“…Indeed, a canonical structural water molecule (30) is predicted to be present in an appropriate position on the trailing chain, bound between the peptide carbonyl group of G22 and the hydroxyl group of O24. Collagen triple helices are highly hydrated (30) and other structural water molecules may also contribute to the SPARCcollagen interaction.…”

Section: Resultsmentioning

confidence: 99%

Structural basis of sequence-specific collagen recognition by SPARC

Hohenester

Sasaki

Giudici

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

124

115

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Protein interactions with the collagen triple helix play a critical role in collagen fibril formation, cell adhesion, and signaling. However, structural insight into sequence-specific collagen recognition is limited to an integrin-peptide complex. A GVMGFO motif in fibrillar collagens (O denotes 4-hydroxyproline) binds 3 unrelated proteins: von Willebrand factor (VWF), discoidin domain receptor 2 (DDR2), and the extracellular matrix protein SPARC/osteonectin/BM-40. We report the crystal structure at 3.2 Å resolution of human SPARC bound to a triple-helical 33-residue peptide harboring the promiscuous GVMGFO motif. SPARC recognizes the GVMGFO motifs of the middle and trailing collagen chains, burying a total of 720 Å 2 of solvent-accessible collagen surface. SPARC binding does not distort the canonical triple helix of the collagen peptide. In contrast, a critical loop in SPARC is substantially remodelled upon collagen binding, creating a deep pocket that accommodates the phenylalanine residue of the trailing collagen chain (''Phe pocket''). This highly restrictive specificity pocket is shared with the collagenbinding integrin I-domains but differs strikingly from the shallow collagen-binding grooves of the platelet receptor glycoprotein VI and microbial adhesins. We speculate that binding of the GVMGFO motif to VWF and DDR2 also results in structural changes and the formation of a Phe pocket. extracellular matrix ͉ X-ray crystallography C ollagen, the most abundant protein in vertebrates, is characterized by a triple-helical structure of 3 polypeptide chains containing repetitive glycine-X-XЈ triplets; the X and XЈ positions, respectively, are often occupied by the imino acids proline and 4-hydroxyproline (O). The 28 human collagens have numerous essential functions in tissue formation, stability and homeostasis, and mutations in collagen genes cause many human diseases (1). Collagens I-III, V and XI form supramolecular fibrils that lend mechanical stability to the vertebrate body. Normal collagen fibrillogenesis in vivo requires a number of globular proteins interacting with the triple helix, such as small leucine-rich repeat proteoglycans (2). Cellular interactions with collagen are mediated by a diverse group of transmembrane collagen receptors, including integrins, discoidin domain receptors (DDRs) and members of the Ig superfamily (3-5). Although the structure of the collagen triple helix has been known for Ͼ50 years (6), protein-collagen interactions remain poorly understood at the atomic level.Synthetic triple-helical peptides have been invaluable in mapping specific binding sites within collagen (7). The major integrin-binding site in fibrillar collagens I and II is a GFOGER motif (8, 9). The atomic details of this important interaction were revealed by a crystal structure of the integrin ␣2 I-domain bound to a 21-residue triple helical peptide, providing the only example to date of a vertebrate protein-collagen complex (10). More recent studies have identified a GVMGFO motif, conserved in collagens I-III...

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Section: Resultsmentioning

confidence: 99%

Structural basis of sequence-specific collagen recognition by SPARC

Hohenester

Sasaki

Giudici

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

124

115

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“…Nevertheless, they do not seem to be small enough to penetrate the nanometric voids between collagen molecules within the demineralized collagen fibers. 50 Moreover, it has been shown that collagen molecules are surrounded by water molecules to form highly ordered and multilayered cylinders of hydration 51 which may favor the hydrolytic degradation of resin monomers in a sub-micrometer level.…”

Section: Why Do Adhesive Interfaces Fail?mentioning

confidence: 99%

Bonding efficiency and durability: current possibilities

et al. 2017

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Bonding plays a major role in dentistry nowadays. Dental adhesives are used in association with composites to solve many restorative issues. However, the wide variety of bonding agents currently available makes it difficult for clinicians to choose the best alternative in terms of material and technique, especially when different clinical situations are considered. Moreover, although bonding agents allow for a more conservative restorative approach, achieving a durable adhesive interface remains a matter of concern, and this mainly due to degradation of the bonding complex in the challenging oral environment. This review aims to present strategies that are being used or those still in development which may help to prevent degradation. It is fundamental that professionals are aware of these strategies to counteract degradation as much as possible. None of them are efficient to completely solve this problem, but they certainly represent reasonable alternatives to increase the lifetime of adhesive restorations.

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“…21,22 These hydrogen bonded networks often adopt pentagonal arrangements of water and are anchored to the peptide chain through backbone carbonyls and hydroxyl groups of Hyp ( Figure 1a). The observation of Hyp involvement in a hydrogen-bonded water network is consistent with that proposed by Ramachandran's group on the basis of modeling and Privalov on the basis of calorimetry studies on collagens.…”

Section: X-ray Crystallography Of Triple-helical Peptidesmentioning

confidence: 99%

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

et al. 2008

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Peptides have been an integral part of the collagen triple‐helix structure story, and have continued to serve as useful models for biophysical studies and for establishing biologically important sequence‐structure‐function relationships. High resolution structures of triple‐helical peptides have confirmed the basic Ramachandran triple‐helix model and provided new insights into the hydration, hydrogen bonding, and sequence dependent helical parameters in collagen. The dependence of collagen triple‐helix stability on the residues in its (Gly‐X‐Y)n repeating sequence has been investigated by measuring melting temperatures of host‐guest peptides and an on‐line collagen stability calculator is now available. Although the presence of Gly as every third residue is essential for an undistorted structure, interruptions in the repeating (Gly‐X‐Y)n amino acid sequence pattern are found in the triple‐helical domains of all nonfibrillar collagens, and are likely to play a role in collagen binding and degradation. Peptide models indicate that small interruptions can be incorporated into a rod‐like triple‐helix with a highly localized effect, which perturbs hydrogen bonds and places the standard triple‐helices on both ends out of register. In contrast to natural interruptions, missense mutations which replace one Gly in a triple‐helix domain by a larger residue have pathological consequences, and studies on peptides containing such Gly substitutions clarify their effect on conformation, stability, and folding. Recent studies suggest peptides may also be useful in defining the basic principles of collagen self‐association to the supramolecular structures found in tissues. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 345–353, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Hydration structure of a collagen peptide

Cited by 582 publications

References 41 publications

Structural basis of sequence-specific collagen recognition by SPARC

Structural basis of sequence-specific collagen recognition by SPARC

Bonding efficiency and durability: current possibilities

Triple‐helical peptides: An approach to collagen conformation, stability, and self‐association

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