Designing phenylalanine-based hybrid biological materials: Controlling morphology: Via molecular composition

Srinivas Mushnoori; Kassandra Schmidt; Vikas Nanda; Meenakshi Dutt

doi:10.1039/c8ob00130h

Designing phenylalanine-based hybrid biological materials: Controlling morphology: Via molecular composition

Srinivas Mushnoori, Kassandra Schmidt, Vikas Nanda, Meenakshi Dutt

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

Harnessing the self-assembly of peptide sequences has demonstrated great promise in the domain of creating high precision shape-tunable biomaterials. The unique properties of peptides allow for a building block approach to material design. In this study, self-assembly of mixed systems encompassing two peptide sequences with identical hydrophobic regions and distinct polar segments is investigated. The two peptide sequences are diphenylalanine and phenylalanine-asparagine-phenylalanine. The study examines the impact of molecular composition (namely, the total peptide concentration and the relative tripeptide concentration) on the morphology of the self-assembled hybrid biological material. We report a rich polymorphism in the assemblies of these peptides and explain the relationship between the peptide sequence, concentration and the morphology of the supramolecular assembly.

Original language	English (US)
Pages (from-to)	2499-2507
Number of pages	9
Journal	Organic and Biomolecular Chemistry
Volume	16
Issue number	14
DOIs	https://doi.org/10.1039/c8ob00130h
State	Published - 2018
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1039/c8ob00130h

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title = "Designing phenylalanine-based hybrid biological materials: Controlling morphology: Via molecular composition",

abstract = "Harnessing the self-assembly of peptide sequences has demonstrated great promise in the domain of creating high precision shape-tunable biomaterials. The unique properties of peptides allow for a building block approach to material design. In this study, self-assembly of mixed systems encompassing two peptide sequences with identical hydrophobic regions and distinct polar segments is investigated. The two peptide sequences are diphenylalanine and phenylalanine-asparagine-phenylalanine. The study examines the impact of molecular composition (namely, the total peptide concentration and the relative tripeptide concentration) on the morphology of the self-assembled hybrid biological material. We report a rich polymorphism in the assemblies of these peptides and explain the relationship between the peptide sequence, concentration and the morphology of the supramolecular assembly.",

author = "Srinivas Mushnoori and Kassandra Schmidt and Vikas Nanda and Meenakshi Dutt",

note = "Funding Information: The authors gratefully acknowledge computational resources provided by the eXtreme Science and Engineering Discovery Environment (XSEDE) allocation TG-DMR140125, and the San Diego Supercomputing Center (SDSC). The authors would like to thank Daniel Grisham and Tianyou Mou for insightful discussions on the study. SM acknowledges the Molecular Sciences Software Institute (MolSSI) for their support. KS would like to thank and acknowledge the New Jersey Space Grant Consortium for their support. MD gratefully acknowledges financial support from NSF CAREER-1654325. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2018.",

year = "2018",

doi = "10.1039/c8ob00130h",

language = "English (US)",

volume = "16",

pages = "2499--2507",

journal = "Organic and Biomolecular Chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

number = "14",

}

TY - JOUR

T1 - Designing phenylalanine-based hybrid biological materials

T2 - Controlling morphology: Via molecular composition

AU - Mushnoori, Srinivas

AU - Schmidt, Kassandra

AU - Nanda, Vikas

AU - Dutt, Meenakshi

N1 - Funding Information: The authors gratefully acknowledge computational resources provided by the eXtreme Science and Engineering Discovery Environment (XSEDE) allocation TG-DMR140125, and the San Diego Supercomputing Center (SDSC). The authors would like to thank Daniel Grisham and Tianyou Mou for insightful discussions on the study. SM acknowledges the Molecular Sciences Software Institute (MolSSI) for their support. KS would like to thank and acknowledge the New Jersey Space Grant Consortium for their support. MD gratefully acknowledges financial support from NSF CAREER-1654325. Publisher Copyright: © The Royal Society of Chemistry 2018.

PY - 2018

Y1 - 2018

N2 - Harnessing the self-assembly of peptide sequences has demonstrated great promise in the domain of creating high precision shape-tunable biomaterials. The unique properties of peptides allow for a building block approach to material design. In this study, self-assembly of mixed systems encompassing two peptide sequences with identical hydrophobic regions and distinct polar segments is investigated. The two peptide sequences are diphenylalanine and phenylalanine-asparagine-phenylalanine. The study examines the impact of molecular composition (namely, the total peptide concentration and the relative tripeptide concentration) on the morphology of the self-assembled hybrid biological material. We report a rich polymorphism in the assemblies of these peptides and explain the relationship between the peptide sequence, concentration and the morphology of the supramolecular assembly.

AB - Harnessing the self-assembly of peptide sequences has demonstrated great promise in the domain of creating high precision shape-tunable biomaterials. The unique properties of peptides allow for a building block approach to material design. In this study, self-assembly of mixed systems encompassing two peptide sequences with identical hydrophobic regions and distinct polar segments is investigated. The two peptide sequences are diphenylalanine and phenylalanine-asparagine-phenylalanine. The study examines the impact of molecular composition (namely, the total peptide concentration and the relative tripeptide concentration) on the morphology of the self-assembled hybrid biological material. We report a rich polymorphism in the assemblies of these peptides and explain the relationship between the peptide sequence, concentration and the morphology of the supramolecular assembly.

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EP - 2507

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 14

ER -

Designing phenylalanine-based hybrid biological materials: Controlling morphology: Via molecular composition

Abstract

All Science Journal Classification (ASJC) codes

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