Controlling oligomerization of pharmaceutical proteins

Catherine H. Schein

doi:10.1016/0031-6865(94)90012-4

Controlling oligomerization of pharmaceutical proteins

Catherine H. Schein

Research output: Contribution to journal › Review article › peer-review

8 Scopus citations

Abstract

The degree of oligomerization (or in some cases aggregation) often determines the physiological half-life and uptake rate of a protein preparation. High-resolution crystal structures of insulin and other pharmacologically interesting proteins have aided in the design of mutants with altered quaternary structure and physiological uptake rates. Analysis of the contacts between natural oligomers and protein complexes can indicate sequences that may enhance protein oligomerization. These sequences can be altered to produce monomeric protein.

Original language	English (US)
Pages (from-to)	119-126
Number of pages	8
Journal	Pharmaceutica Acta Helvetiae
Volume	69
Issue number	3
DOIs	https://doi.org/10.1016/0031-6865(94)90012-4
State	Published - Dec 1994
Externally published	Yes

Keywords

Interprotein contacts
Protein aggregation
Protein oligomerization
Site-directed mutagenesis

ASJC Scopus subject areas

Molecular Medicine
General Pharmacology, Toxicology and Pharmaceutics

Access to Document

10.1016/0031-6865(94)90012-4

Cite this

@article{d148fc58b480438f8697dbd2d92a5a6d,

title = "Controlling oligomerization of pharmaceutical proteins",

abstract = "The degree of oligomerization (or in some cases aggregation) often determines the physiological half-life and uptake rate of a protein preparation. High-resolution crystal structures of insulin and other pharmacologically interesting proteins have aided in the design of mutants with altered quaternary structure and physiological uptake rates. Analysis of the contacts between natural oligomers and protein complexes can indicate sequences that may enhance protein oligomerization. These sequences can be altered to produce monomeric protein.",

keywords = "Interprotein contacts, Protein aggregation, Protein oligomerization, Site-directed mutagenesis",

author = "Schein, {Catherine H.}",

year = "1994",

month = dec,

doi = "10.1016/0031-6865(94)90012-4",

language = "English (US)",

volume = "69",

pages = "119--126",

journal = "Pharmaceutica Acta Helvetiae",

issn = "0031-6865",

publisher = "Elsevier B.V.",

number = "3",

}

TY - JOUR

T1 - Controlling oligomerization of pharmaceutical proteins

AU - Schein, Catherine H.

PY - 1994/12

Y1 - 1994/12

N2 - The degree of oligomerization (or in some cases aggregation) often determines the physiological half-life and uptake rate of a protein preparation. High-resolution crystal structures of insulin and other pharmacologically interesting proteins have aided in the design of mutants with altered quaternary structure and physiological uptake rates. Analysis of the contacts between natural oligomers and protein complexes can indicate sequences that may enhance protein oligomerization. These sequences can be altered to produce monomeric protein.

AB - The degree of oligomerization (or in some cases aggregation) often determines the physiological half-life and uptake rate of a protein preparation. High-resolution crystal structures of insulin and other pharmacologically interesting proteins have aided in the design of mutants with altered quaternary structure and physiological uptake rates. Analysis of the contacts between natural oligomers and protein complexes can indicate sequences that may enhance protein oligomerization. These sequences can be altered to produce monomeric protein.

KW - Interprotein contacts

KW - Protein aggregation

KW - Protein oligomerization

KW - Site-directed mutagenesis

UR - http://www.scopus.com/inward/record.url?scp=0028569551&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028569551&partnerID=8YFLogxK

U2 - 10.1016/0031-6865(94)90012-4

DO - 10.1016/0031-6865(94)90012-4

M3 - Review article

C2 - 7846082

AN - SCOPUS:0028569551

SN - 0031-6865

VL - 69

SP - 119

EP - 126

JO - Pharmaceutica Acta Helvetiae

JF - Pharmaceutica Acta Helvetiae

IS - 3

ER -

Controlling oligomerization of pharmaceutical proteins

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this