A mathematical model to predict the partitioning of peptides and peptide-modified proteins in aqueous two-phase systems

dc.contributor.author	Eiteman, MA	en
dc.contributor.author	Hassinen, C	en
dc.contributor.author	Veide, A	en
dc.date.accessioned	2014-06-06T06:42:32Z
dc.date.available	2014-06-06T06:42:32Z
dc.date.issued	1994	en
dc.identifier.issn	87567938	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/674
dc.relation.uri	http://www.scopus.com/inward/record.url?eid=2-s2.0-0028501220&partnerID=40&md5=a13068b7f079b017d13855f850cf183d	en
dc.subject.other	Amino acids	en
dc.subject.other	Forecasting	en
dc.subject.other	Mathematical models	en
dc.subject.other	Proteins	en
dc.subject.other	Separation	en
dc.subject.other	Hydrophobicity	en
dc.subject.other	Partitioning	en
dc.subject.other	Peptides	en
dc.subject.other	Polypeptides	en
dc.subject.other	immunoglobulin G	en
dc.subject.other	oligopeptide	en
dc.subject.other	staphylococcus protein A	en
dc.subject.other	water	en
dc.subject.other	amino acid sequence	en
dc.subject.other	article	en
dc.subject.other	binding site	en
dc.subject.other	chemical model	en
dc.subject.other	chemistry	en
dc.subject.other	isoelectric point	en
dc.subject.other	isolation and purification	en
dc.subject.other	mathematics	en
dc.subject.other	metabolism	en
dc.subject.other	molecular genetics	en
dc.subject.other	pH	en
dc.subject.other	physical chemistry	en
dc.subject.other	Amino Acid Sequence	en
dc.subject.other	Binding Sites	en
dc.subject.other	Chemistry, Physical	en
dc.subject.other	Hydrogen-Ion Concentration	en
dc.subject.other	Immunoglobulin G	en
dc.subject.other	Isoelectric Point	en
dc.subject.other	Mathematics	en
dc.subject.other	Models, Chemical	en
dc.subject.other	Molecular Sequence Data	en
dc.subject.other	Oligopeptides	en
dc.subject.other	Staphylococcal Protein A	en
dc.subject.other	Support, Non-U.S. Gov't	en
dc.subject.other	Water	en
dc.title	A mathematical model to predict the partitioning of peptides and peptide-modified proteins in aqueous two-phase systems	en
heal.type	journalArticle	en
heal.publicationDate	1994	en
heal.abstract	A mathematical procedure was developed to predict the partition coefficients of the peptides AIIP, AWWP, AIIPAIIP and AWWPAWWP in polyethylene glycol) (PEG)/ phosphate aqueous two-phase systems from amino acid hydrophobicities. In general, peptides containing tryptophan partition more into the PEG-enriched upper phase than analogous peptides containing isoleucine. Specifically, as the PEG concentration difference between the phases increased in a PEG/potassium phosphate aqueous two-phase system, the peptide AIIP was observed to have a partition coefficient ranging from 1.2 to 1.6, AIIPAIIP from 2.4 to 5.7, AWWP from 13.5 to 32.2, and AWWPAWWP from 43 to 170. The model was extended to predict the partitioning of a staphylococcal protein A derivative (ZZ) modified with these four peptides. As predicted, the protein modified with isoleucine-containing peptides had lower partition coefficients than the protein modified with tryptophan-containing peptides. The partition coefficient of the ZZ protein ranged from 0.35 to 0.20, that of ZZAIIPAIIP from 0.58 to 0.48, and that of ZZAWWPAWWP from 3.5 to 5.3 in these systems. The results show that short peptide handles can significantly enhance the partitioning of proteins in aqueous two-phase systems. The relationship between the model and the surface exposure of peptide handles and the utility of the model to aid in the design of such handles to enhance purifications are also discussed. © 1994 American Chemical Society and American Institute of Chemical Engineers.	en
heal.journalName	Biotechnology Progress	en
dc.identifier.issue	5	en
dc.identifier.volume	10	en
dc.identifier.spage	513	en
dc.identifier.epage	519	en