Nature's complex copolymers: Engineering design of oligopeptide materials

Michael Caplan, Douglas A. Lauffenburger

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Proteins evolved in nature can form precise structures exhibiting nanometer-length-scale features that have great potential for industrial application. However, many of these applications remain unrealized because of limitations in combinatorial and directed evolutionary approaches. An alternative approach that might be able to overcome these limitations is rational design of protein (or oligopeptide in the case of <50 amino acid) sequences. This article reviews the advances that have been made in understanding the protein sequence/structure problem by starting with "simple", repetitive sequences and building desired complexity. The review is paralleled by a discussion of micelle, colloid, and block copolymer literature to provide a polymer science context for understanding the protein-folding problem. We note that pentapeptide repeat units provide a useful definition of hydrophobicity, the key determinant of secondary structure, by causing the protein backbone to twist in order to become amphiphilic. Heptad repeating α-helices and hydrophobic-charged/polar-hydrophobic-charged/polar repeating β-sheets show that these amphiphiles can be driven into tertiary structures similarly to surfactants forming micelles. We describe how electrostatic charges can provide specificity for structure and assembly conditions. Finally, we provide several examples of protein materials that have been rationally designed using these principles.

Original languageEnglish (US)
Pages (from-to)403-412
Number of pages10
JournalIndustrial and Engineering Chemistry Research
Volume41
Issue number3
StatePublished - Feb 6 2002
Externally publishedYes

Fingerprint

Oligopeptides
Copolymers
Proteins
engineering
protein
Micelles
Protein folding
Amphiphiles
Colloids
Hydrophobicity
secondary structure
Surface-Active Agents
Microsatellite Repeats
Block copolymers
Industrial applications
hydrophobicity
Amino acids
colloid
Electrostatics
Polymers

ASJC Scopus subject areas

  • Polymers and Plastics
  • Environmental Science(all)
  • Chemical Engineering (miscellaneous)

Cite this

Nature's complex copolymers : Engineering design of oligopeptide materials. / Caplan, Michael; Lauffenburger, Douglas A.

In: Industrial and Engineering Chemistry Research, Vol. 41, No. 3, 06.02.2002, p. 403-412.

Research output: Contribution to journalArticle

Caplan, Michael ; Lauffenburger, Douglas A. / Nature's complex copolymers : Engineering design of oligopeptide materials. In: Industrial and Engineering Chemistry Research. 2002 ; Vol. 41, No. 3. pp. 403-412.
@article{5a69ebe0e5eb4e579fa88882e51b7195,
title = "Nature's complex copolymers: Engineering design of oligopeptide materials",
abstract = "Proteins evolved in nature can form precise structures exhibiting nanometer-length-scale features that have great potential for industrial application. However, many of these applications remain unrealized because of limitations in combinatorial and directed evolutionary approaches. An alternative approach that might be able to overcome these limitations is rational design of protein (or oligopeptide in the case of <50 amino acid) sequences. This article reviews the advances that have been made in understanding the protein sequence/structure problem by starting with {"}simple{"}, repetitive sequences and building desired complexity. The review is paralleled by a discussion of micelle, colloid, and block copolymer literature to provide a polymer science context for understanding the protein-folding problem. We note that pentapeptide repeat units provide a useful definition of hydrophobicity, the key determinant of secondary structure, by causing the protein backbone to twist in order to become amphiphilic. Heptad repeating α-helices and hydrophobic-charged/polar-hydrophobic-charged/polar repeating β-sheets show that these amphiphiles can be driven into tertiary structures similarly to surfactants forming micelles. We describe how electrostatic charges can provide specificity for structure and assembly conditions. Finally, we provide several examples of protein materials that have been rationally designed using these principles.",
author = "Michael Caplan and Lauffenburger, {Douglas A.}",
year = "2002",
month = "2",
day = "6",
language = "English (US)",
volume = "41",
pages = "403--412",
journal = "Industrial & Engineering Chemistry Product Research and Development",
issn = "0019-7890",
publisher = "American Chemical Society",
number = "3",

}

TY - JOUR

T1 - Nature's complex copolymers

T2 - Engineering design of oligopeptide materials

AU - Caplan, Michael

AU - Lauffenburger, Douglas A.

PY - 2002/2/6

Y1 - 2002/2/6

N2 - Proteins evolved in nature can form precise structures exhibiting nanometer-length-scale features that have great potential for industrial application. However, many of these applications remain unrealized because of limitations in combinatorial and directed evolutionary approaches. An alternative approach that might be able to overcome these limitations is rational design of protein (or oligopeptide in the case of <50 amino acid) sequences. This article reviews the advances that have been made in understanding the protein sequence/structure problem by starting with "simple", repetitive sequences and building desired complexity. The review is paralleled by a discussion of micelle, colloid, and block copolymer literature to provide a polymer science context for understanding the protein-folding problem. We note that pentapeptide repeat units provide a useful definition of hydrophobicity, the key determinant of secondary structure, by causing the protein backbone to twist in order to become amphiphilic. Heptad repeating α-helices and hydrophobic-charged/polar-hydrophobic-charged/polar repeating β-sheets show that these amphiphiles can be driven into tertiary structures similarly to surfactants forming micelles. We describe how electrostatic charges can provide specificity for structure and assembly conditions. Finally, we provide several examples of protein materials that have been rationally designed using these principles.

AB - Proteins evolved in nature can form precise structures exhibiting nanometer-length-scale features that have great potential for industrial application. However, many of these applications remain unrealized because of limitations in combinatorial and directed evolutionary approaches. An alternative approach that might be able to overcome these limitations is rational design of protein (or oligopeptide in the case of <50 amino acid) sequences. This article reviews the advances that have been made in understanding the protein sequence/structure problem by starting with "simple", repetitive sequences and building desired complexity. The review is paralleled by a discussion of micelle, colloid, and block copolymer literature to provide a polymer science context for understanding the protein-folding problem. We note that pentapeptide repeat units provide a useful definition of hydrophobicity, the key determinant of secondary structure, by causing the protein backbone to twist in order to become amphiphilic. Heptad repeating α-helices and hydrophobic-charged/polar-hydrophobic-charged/polar repeating β-sheets show that these amphiphiles can be driven into tertiary structures similarly to surfactants forming micelles. We describe how electrostatic charges can provide specificity for structure and assembly conditions. Finally, we provide several examples of protein materials that have been rationally designed using these principles.

UR - http://www.scopus.com/inward/record.url?scp=0037028657&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037028657&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0037028657

VL - 41

SP - 403

EP - 412

JO - Industrial & Engineering Chemistry Product Research and Development

JF - Industrial & Engineering Chemistry Product Research and Development

SN - 0019-7890

IS - 3

ER -