Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres

Yao, Linyan; He, Manman; Li, Dongfang; Tian, Jing; Liu, Huanxiang; Xiao, Jianxi

doi:10.1039/c7ra11855d

Cited by 10 publications

(4 citation statements)

References 46 publications

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“…The sequence of bovine type III collagen corresponding to residues 538–570 was selected since this sequence was detected with or without affinity purification of glyoxal-modified collagen. The type III collagen sequences containing GXXGER motifs that are recognized by integrin were also selected, and both the N- and C-termini of four peptides composed of nine residues were coupled with (GPO) 4 in order to form a collagen-like helical structure [32, 33]. In addition, the amount of CMA formation in these collagen peptides was compared with the HSA peptide reported as the hotspot of reactive aldehyde-modification in HSA [34].…”

Section: Resultsmentioning

confidence: 99%

N^ω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues

Kinoshita

Mera

Ichikawa

et al. 2019

Oxidative Medicine and Cellular Longevity

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Advanced glycation end products (AGEs) accumulate in proteins during aging in humans. In particular, the AGE structure Nω-(carboxymethyl)arginine (CMA) is produced by oxidation in glycated collagen, accounting for one of the major proteins detected in biological samples. In this study, we investigated the mechanism by which CMA is generated in collagen and detected CMA in collagen-rich tissues. When various protein samples were incubated with glucose, the CMA content, detected using a monoclonal antibody, increased in a time-dependent manner only in glycated collagen, whereas the formation of Nε-(carboxymethyl)lysine (CML), a major antigenic AGE, was detected in all glycated proteins. Dominant CMA formation in glycated collagen was also observed by electrospray ionization-liquid chromatography-tandem mass spectrometry (LC-MS/MS). During incubation of glucose with collagen, CMA formation was enhanced with increasing glucose concentration, whereas it was inhibited in the presence of dicarbonyl-trapping reagents and a metal chelator. CMA formation was also observed upon incubating collagen with glyoxal, and CMA was generated in a time-dependent manner when glyoxal was incubated with type I–IV collagens. To identify hotspots of CMA formation, tryptic digests of glycated collagen were applied to an affinity column conjugated with anti-CMA. Several CMA peptides that are important for recognition by integrins were detected by LC-MS/MS and amino acid sequence analyses. CMA formation on each sequence was confirmed by incubation of the synthesized peptides with glyoxal and ribose. LC-MS detected CMA in the mouse skin at a higher level than other AGEs. Furthermore, CMA accumulation was greater in the human aorta of older individuals. Overall, our study provides evidence that CMA is a representative AGE structure that serves as a useful index to reflect the oxidation and glycation of collagen.

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Section: Resultsmentioning

confidence: 99%

N^ω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues

Kinoshita

Mera

Ichikawa

et al. 2019

Oxidative Medicine and Cellular Longevity

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“…These studies highlight the utility of nonequilibrium processing on hierarchical self-assembly of synthetic peptides. Rational molecular design of CMPs to promote their assembly into highly ordered nanofibers, hydrogels, vesicles, and nanospheres have also been demonstrated. − …”

Section: Peptide Self-assemblymentioning

confidence: 99%

Peptide Design and Self-assembly into Targeted Nanostructure and Functional Materials

et al. 2021

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Peptides have been extensively utilized to construct nanomaterials that display targeted structure through hierarchical assembly. The self-assembly of both rationally designed peptides derived from naturally occurring domains in proteins as well as intuitively or computationally designed peptides that form β-sheets and helical secondary structures have been widely successful in constructing nanoscale morphologies with well-defined 1-d, 2-d, and 3-d architectures. In this review, we discuss these successes of peptide self-assembly, especially in the context of designing hierarchical materials. In particular, we emphasize the differences in the level of peptide design as an indicator of complexity within the targeted self-assembled materials and highlight future avenues for scientific and technological advances in this field.

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“…In this context, a notable observation was recently reported by Yao et al: they have demonstrated that the addition of polar terminal residues to the CMP scaffold promotes their assembly into a separate phase in water, thereby forming nanospherical particles. 25,26 As the conclusion from our literature survey, there is an unfortunate lack of information on whether CMPs would assemble in a hydrophobic environment, and how the triple helix is maintained under non-aqueous conditions. To this end, we decided to design CMPs with an amplified hydrophobicity of the triple helical exterior, with the idea that this would force the peptides to assemble in nonpolar environments.…”

Section: Introductionmentioning

confidence: 97%

Promotion of the collagen triple helix in a hydrophobic environment

Kubyshkin

Budiša

2019

Org. Biomol. Chem.

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Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres

Abstract: Amphiphile-like collagen mimic peptides with terminal aspartic acids may provide a general and convenient strategy to create well-defined nanostructures.

Cited by 10 publications

References 46 publications

N^ω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues

N^ω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues

Peptide Design and Self-assembly into Targeted Nanostructure and Functional Materials

Promotion of the collagen triple helix in a hydrophobic environment

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Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres

Abstract: Amphiphile-like collagen mimic peptides with terminal aspartic acids may provide a general and convenient strategy to create well-defined nanostructures.

Cited by 10 publications

References 46 publications

Nω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues

Nω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues

Peptide Design and Self-assembly into Targeted Nanostructure and Functional Materials

Promotion of the collagen triple helix in a hydrophobic environment

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Product

Resources

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N^ω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues

N^ω-(Carboxymethyl)arginine Is One of the Dominant Advanced Glycation End Products in Glycated Collagens and Mouse Tissues