“PP-type” self-assembling peptides with superior rheological properties

Li, Fangmin; Gao, Lichang; Zhang, Xudong; Pin, Wang; Liu, Yuanxue; Feng, Jinhui; Zhang, Chunxia; Zhao, Chengru; Zhang, Shang

doi:10.1039/d1na00534k

Cited by 7 publications

(2 citation statements)

References 41 publications

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“…For the RADA family of peptides that self-assemble due to alternating hydrophobic and negatively charged peptides, the effect of adding proline amino acids at both the C-and N-terminals was shown to increase the peptide solubility, sol-gel transition ability and increase the storage modulus through the effect of proline-proline-type self-assembly. These examples illustrate how minor changes to the peptide structure can influence the resulting properties on different scales [12].…”

Section: Introductionmentioning

confidence: 98%

Controlling the self-assembly and material properties of β-sheet peptide hydrogels by modulating intermolecular interactions

Warren

Culbert

Miles

et al. 2023

Preprint

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Self-assembling peptides are a promising biomaterial with potential applications in medical de-vices and drug delivery. In the right combination of conditions, self-assembling peptides can form self-supporting hydrogels. Here, we describe how balancing attractive and repulsive intermo-lecular forces is critical for successful hydrogel formation. Electrostatic repulsion is tuned by al-tering the peptide’s net charge and intermolecular attractions are controlled through the degree of hydrogen bonding between specific amino acid residues. We find that an overall net peptide charge of +/-2 is optimal to facilitate the assembly of self-supporting hydrogels. If the net peptide charge is too low then dense aggregates form, while a high molecular charge inhibits the for-mation of larger structures. At constant charge, altering the terminal amino acids from glutamine to serine decreases the degree of hydrogen bonding within the assembling network. This tunes the viscoelastic properties of the gel, reducing the elastic modulus by two to three orders of magnitude. Finally, hydrogels could be formed from glutamine-rich, highly charged peptides by mixing the peptides in combinations with a resultant net charge of +/-2. These results illustrate how understanding and controlling self-assembly mechanisms through modulating intermolecular interactions can be exploited to derive a range of structures with tuneable properties.

show abstract

Section: Introductionmentioning

confidence: 98%

Controlling the self-assembly and material properties of β-sheet peptide hydrogels by modulating intermolecular interactions

Warren

Culbert

Miles

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

“…For the RADA family of peptides that self-assemble due to alternating hydrophobic and negatively charged peptides, the effect of adding proline amino acids at both the C- and N- terminals was shown to increase the peptide solubility, sol–gel transition ability, and the storage modulus through the effect of proline–proline-type self-assembly. These examples illustrate how minor changes to the peptide structure can influence the resulting properties on different scales [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions

Warren

Culbert

Miles

et al. 2023

Gels

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Self-assembling peptides are a promising biomaterial with potential applications in medical devices and drug delivery. In the right combination of conditions, self-assembling peptides can form self-supporting hydrogels. Here, we describe how balancing attractive and repulsive intermolecular forces is critical for successful hydrogel formation. Electrostatic repulsion is tuned by altering the peptide’s net charge, and intermolecular attractions are controlled through the degree of hydrogen bonding between specific amino acid residues. We find that an overall net peptide charge of +/−2 is optimal to facilitate the assembly of self-supporting hydrogels. If the net peptide charge is too low then dense aggregates form, while a high molecular charge inhibits the formation of larger structures. At a constant charge, altering the terminal amino acids from glutamine to serine decreases the degree of hydrogen bonding within the assembling network. This tunes the viscoelastic properties of the gel, reducing the elastic modulus by two to three orders of magnitude. Finally, hydrogels could be formed from glutamine-rich, highly charged peptides by mixing the peptides in combinations with a resultant net charge of +/−2. These results illustrate how understanding and controlling self-assembly mechanisms through modulating intermolecular interactions can be exploited to derive a range of structures with tuneable properties.

show abstract

Mechanism of Peptide Self-assembly and Its Study in Biomedicine

Yang,

Ma,

et al. 2024

Protein J

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“PP-type” self-assembling peptides with superior rheological properties

Abstract: The ionic-complementary self-assembling peptides discovered by Zhang Shuguang have solution-to-gel (sol-gel) transition capacity and one such peptide RADA16 has been commercialized into hemostatic agents. However, their sol-gel transition ability was...

Cited by 7 publications

References 41 publications

Controlling the self-assembly and material properties of β-sheet peptide hydrogels by modulating intermolecular interactions

Controlling the self-assembly and material properties of β-sheet peptide hydrogels by modulating intermolecular interactions

Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions

Mechanism of Peptide Self-assembly and Its Study in Biomedicine

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