Tuning Oligovalent Biomacromolecular Interfaces Using Double-Layered α-Helical Coiled-Coil Nanoassemblies from Lariat-Type Building Blocks

Woo jin Jeong, Se Hwan Choi, Kyeong Sik Jin, Yong-beom Lim

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The target affinity and selectivity of many biomacromolecules depend on the three-dimensional (3D) distribution of multiple ligands on their surfaces. Here, we devised a self-assembly strategy to control the target-tailored 3D distribution of multiple α-helical ligands on a coiled-coil core scaffold using novel lariat-type supramolecular building blocks. Depending on the coiled-coil composition and ligand grafting sites in the lariat building blocks, the structural and functional features of the self-assembled peptide nanostructures (SPNs) could be variably fine-tuned. Using oligovalent protein-RNA (Rev-RRE) interactions as a model system, we demonstrate that longer grafting reinforces the helicity of the peptide ligands, whereas shorter grafting strengthens the target binding affinity of the SPNs in both monovalent and oligovalent interactions. This supramolecular approach should be useful in developing precisely controllable multivalent ligands for biomacromolecular interactions.

Original languageEnglish
Pages (from-to)1406-1410
Number of pages5
JournalACS Macro Letters
Volume5
Issue number12
DOIs
Publication statusPublished - 2016 Dec 20

Fingerprint

Tuning
Ligands
Peptides
Nanostructures
RNA
Scaffolds
Self assembly
Proteins
Chemical analysis

All Science Journal Classification (ASJC) codes

  • Organic Chemistry
  • Polymers and Plastics
  • Inorganic Chemistry
  • Materials Chemistry

Cite this

@article{8853f239f19247efb8dfa30cb97c9a3f,
title = "Tuning Oligovalent Biomacromolecular Interfaces Using Double-Layered α-Helical Coiled-Coil Nanoassemblies from Lariat-Type Building Blocks",
abstract = "The target affinity and selectivity of many biomacromolecules depend on the three-dimensional (3D) distribution of multiple ligands on their surfaces. Here, we devised a self-assembly strategy to control the target-tailored 3D distribution of multiple α-helical ligands on a coiled-coil core scaffold using novel lariat-type supramolecular building blocks. Depending on the coiled-coil composition and ligand grafting sites in the lariat building blocks, the structural and functional features of the self-assembled peptide nanostructures (SPNs) could be variably fine-tuned. Using oligovalent protein-RNA (Rev-RRE) interactions as a model system, we demonstrate that longer grafting reinforces the helicity of the peptide ligands, whereas shorter grafting strengthens the target binding affinity of the SPNs in both monovalent and oligovalent interactions. This supramolecular approach should be useful in developing precisely controllable multivalent ligands for biomacromolecular interactions.",
author = "Jeong, {Woo jin} and Choi, {Se Hwan} and Jin, {Kyeong Sik} and Yong-beom Lim",
year = "2016",
month = "12",
day = "20",
doi = "10.1021/acsmacrolett.6b00746",
language = "English",
volume = "5",
pages = "1406--1410",
journal = "ACS Macro Letters",
issn = "2161-1653",
publisher = "American Chemical Society",
number = "12",

}

Tuning Oligovalent Biomacromolecular Interfaces Using Double-Layered α-Helical Coiled-Coil Nanoassemblies from Lariat-Type Building Blocks. / Jeong, Woo jin; Choi, Se Hwan; Jin, Kyeong Sik; Lim, Yong-beom.

In: ACS Macro Letters, Vol. 5, No. 12, 20.12.2016, p. 1406-1410.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Tuning Oligovalent Biomacromolecular Interfaces Using Double-Layered α-Helical Coiled-Coil Nanoassemblies from Lariat-Type Building Blocks

AU - Jeong, Woo jin

AU - Choi, Se Hwan

AU - Jin, Kyeong Sik

AU - Lim, Yong-beom

PY - 2016/12/20

Y1 - 2016/12/20

N2 - The target affinity and selectivity of many biomacromolecules depend on the three-dimensional (3D) distribution of multiple ligands on their surfaces. Here, we devised a self-assembly strategy to control the target-tailored 3D distribution of multiple α-helical ligands on a coiled-coil core scaffold using novel lariat-type supramolecular building blocks. Depending on the coiled-coil composition and ligand grafting sites in the lariat building blocks, the structural and functional features of the self-assembled peptide nanostructures (SPNs) could be variably fine-tuned. Using oligovalent protein-RNA (Rev-RRE) interactions as a model system, we demonstrate that longer grafting reinforces the helicity of the peptide ligands, whereas shorter grafting strengthens the target binding affinity of the SPNs in both monovalent and oligovalent interactions. This supramolecular approach should be useful in developing precisely controllable multivalent ligands for biomacromolecular interactions.

AB - The target affinity and selectivity of many biomacromolecules depend on the three-dimensional (3D) distribution of multiple ligands on their surfaces. Here, we devised a self-assembly strategy to control the target-tailored 3D distribution of multiple α-helical ligands on a coiled-coil core scaffold using novel lariat-type supramolecular building blocks. Depending on the coiled-coil composition and ligand grafting sites in the lariat building blocks, the structural and functional features of the self-assembled peptide nanostructures (SPNs) could be variably fine-tuned. Using oligovalent protein-RNA (Rev-RRE) interactions as a model system, we demonstrate that longer grafting reinforces the helicity of the peptide ligands, whereas shorter grafting strengthens the target binding affinity of the SPNs in both monovalent and oligovalent interactions. This supramolecular approach should be useful in developing precisely controllable multivalent ligands for biomacromolecular interactions.

UR - http://www.scopus.com/inward/record.url?scp=85006998836&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85006998836&partnerID=8YFLogxK

U2 - 10.1021/acsmacrolett.6b00746

DO - 10.1021/acsmacrolett.6b00746

M3 - Article

AN - SCOPUS:85006998836

VL - 5

SP - 1406

EP - 1410

JO - ACS Macro Letters

JF - ACS Macro Letters

SN - 2161-1653

IS - 12

ER -