Investigation of pH‐Dependent Collagen Triple‐Helix Formation

Lee, Song-Gil; Lee, Jee Yeon; Chmielewski, Jean

doi:10.1002/anie.200802224

Cited by 28 publications

(17 citation statements)

References 28 publications

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“…However, acetyl-[Pro-Hyp(CO 2 )-Gly] 7 -OH formed a triple-helix with a T m = 17 ° C at pH 2.7 but had no triple-helical structure at pH 7.2. 42 pH-dependent triple-helical stability was also observed for (Pro-4 R -Amp-Gly) 6 sequences, where 4 R -Amp is (2 S ,4 R )-4-aminoproline. 43,44 Modification of the sequence (Gly-Pro-Hyp) 3 -Gly-Cys-Hyp-Gly-Pro-Hyp-Gly-Pro-Cys-(Gly-Pro-Hyp) 5 -Gly-Gly-NH 2 with an azobenzene bridge between the Cys residues resulted in a THP whose stability decreased up irradiation at λ = 330 nm at 27 ° C. 45 Unfortunately, the poor solubility of this peptide prohibited quantitative analysis of its stability.…”

Section: Associated Triple-helical Peptidesmentioning

confidence: 71%

“…To create a triple-helix that was pH dependent, Hyp was modified by addition of a carboxylate by O-alkylation. 42 Interestingly, the incorporation of 1 or 3 Hyp(CO 2 ) residues within a Pro-Hyp-Gly template did not result in a pH-sensitive triple-helix. However, acetyl-[Pro-Hyp(CO 2 )-Gly] 7 -OH formed a triple-helix with a T m = 17 ° C at pH 2.7 but had no triple-helical structure at pH 7.2.…”

Section: Associated Triple-helical Peptidesmentioning

confidence: 99%

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Synthesis and biological applications of collagen-model triple-helical peptides

Fields¹

2010

Org. Biomol. Chem.

117

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Triple-helical peptides (THPs) have been utilized as collagen models since the 1960s. The original focus for THP-based research was to unravel the structural determinants of collagen. In the last two decades, virtually all aspects of collagen structural biochemistry have been explored with THP models. More specifically, secondary amino acid analogs have been incorporated into THPs to more fully understand the forces that stabilize triple-helical structure. Heterotrimeric THPs have been utilized to better appreciate the contributions of chain sequence diversity on collagen function. The role of collagen as a cell signaling protein has been dissected using THPs that represent ligands for specific receptors. The mechanisms of collagenolysis have been investigated using THP substrates and inhibitors. Finally, THPs have been developed for biomaterial applications. These aspects of THP-based research are overviewed herein.

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Section: Associated Triple-helical Peptidesmentioning

confidence: 71%

Section: Associated Triple-helical Peptidesmentioning

confidence: 99%

Synthesis and biological applications of collagen-model triple-helical peptides

Fields¹

2010

Org. Biomol. Chem.

117

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“…Prior study has demonstrated that interhelical electrostatic repulsion arising from deprotonated carboxylates under neutral conditions disfavors triple‐helix formation in the absence of Hyp hydroxy groups 9a. However, we hypothesized that this pH‐dependent folding tendency would be reversed if carboxylate groups were linked to hydrogen‐bond donors (Hyp residues) in adjacent strands.…”

Section: Methodsmentioning

confidence: 88%

Elucidating pH‐Dependent Collagen Triple Helix Formation through Interstrand Hydroxyproline‐Glutamic Acid Interactions

et al. 2014

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Here, we describe systematic explorations into the molecular basis underlying hydroxyproline-mediated interstrand interactions on the triple-helical stability of collagen-mimetic peptides containing glutamic acid residues. Our studies reveal that the triple-helical stability of these peptides relies on the existence of interstrand interactions between hydroxyprolines and glutamic acid residues that are pH dependent. These unique interactions have been used to engineer collagen peptides that form triple helices on demand through pH control.

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“…To create a triple-helix that was pH dependent, Hyp was modified by O -alkylation to a carboxylate group [39]. The incorporation of 1 or 3 Hyp(CO 2 ) residues within a Pro-Hyp-Gly template did not result in a pH-sensitive triple-helix.…”

Section: Introductionmentioning

confidence: 99%

“…The incorporation of 1 or 3 Hyp(CO 2 ) residues within a Pro-Hyp-Gly template did not result in a pH-sensitive triple-helix. However, acetyl-[Pro-Hyp(CO 2 )-Gly] 7 -OH formed a triple-helix with a T m = 17 °C at pH 2.7 but had no triple-helical structure at pH 7.2 [39]. pH-dependent triple-helical stability was also observed for (Pro-4 R- Amp-Gly) 6 sequences, where 4 R -Amp is (2 S ,4 R )-4-aminoproline [40, 41].…”

Section: Introductionmentioning

confidence: 99%

Stabilization of Collagen-Model, Triple-Helical Peptides for In Vitro and In Vivo Applications

Bhowmick

Fields

2013

Methods in Molecular Biology

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The triple-helical structure of collagen has been accurately reproduced in numerous chemical and recombinant model systems. Triple-helical peptides and proteins have found application for dissecting collagen-stabilizing forces, isolating receptor- and protein-binding sites in collagen, mechanistic examination of collagenolytic proteases, and development of novel biomaterials. Introduction of native-like sequences into triple-helical constructs can reduce the thermal stability of the triple-helix to below that of the physiological environment. In turn, incorporation of nonnative amino acids and/or templates can enhance triple-helix stability. We presently describe approaches by which triple-helical structure can be modulated for use under physiological or near-physiological conditions.

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Investigation of pH‐Dependent Collagen Triple‐Helix Formation

Cited by 28 publications

References 28 publications

Synthesis and biological applications of collagen-model triple-helical peptides

Synthesis and biological applications of collagen-model triple-helical peptides

Elucidating pH‐Dependent Collagen Triple Helix Formation through Interstrand Hydroxyproline‐Glutamic Acid Interactions

Stabilization of Collagen-Model, Triple-Helical Peptides for In Vitro and In Vivo Applications

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