PubTransformer

A site to transform Pubmed publications into these bibliographic reference formats: ADS, BibTeX, EndNote, ISI used by the Web of Knowledge, RIS, MEDLINE, Microsoft's Word 2007 XML.

Utilization of Zwitterion-based solutions to dissect the relative effects of solution pH and ionic strength on the aggregation behavior and conformational stability of a fusion protein.

Abstract Solution pH and ionic strength (I) have complex effects on protein stability. We developed an experimental approach based on exploitation of the zwitterionic characteristic of amino acid molecules to probe the relative contribution from each. A variety of types of amino acid solutions were adopted to investigate the effects of pH and I in a manner that allows independent evaluation of each factor. The same effect could not be achieved using conventional buffer solutions. Size-exclusion chromatography, capillary differential scanning calorimetry, and fluorescence spectroscopy were utilized to probe the protein aggregation and conformation. The results suggested that, in addition to pH, solution ionic strength as a function of ionization state of the amino acid molecules and the ions introduced by pH adjustment played an important role in the aggregation and conformation of the protein studied. This experimental approach offers a useful tool to aid fundamental understanding of the relative effects of solution pH and ionic strength on protein stability.
PMID
Related Publications

Basal buffer systems for a newly glycosylated recombinant human interferon-? with biophysical stability and DoE approaches.

Self-aggregation of a recombinant form of the propeptide NH2-terminal of the precursor of pulmonary surfactant protein SP-B: a conformational study.

Solution behavior of IFN-beta-1a: an empirical phase diagram based approach.

Characteristic properties of proteins from pre-ecdysial cuticle of larvae and pupae of the mealworm Tenebrio molitor.

Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies.

Authors

Mayor MeshTerms

Hydrogen-Ion Concentration

Osmolar Concentration

Keywords

calorimetry (DSC)

chromatography

fluorescence spectroscopy

ionic strength

pH

protein aggregation

protein structure

zwitterion

Journal Title journal of pharmaceutical sciences
Publication Year Start
%A Zhou, Rong; Nashine, Vishal; Palm, Thomas; Gandhi, Rajesh; Adams, Monica
%T Utilization of Zwitterion-based solutions to dissect the relative effects of solution pH and ionic strength on the aggregation behavior and conformational stability of a fusion protein.
%J Journal of pharmaceutical sciences, vol. 103, no. 10, pp. 3065-3074
%D 10/2014
%V 103
%N 10
%M eng
%B Solution pH and ionic strength (I) have complex effects on protein stability. We developed an experimental approach based on exploitation of the zwitterionic characteristic of amino acid molecules to probe the relative contribution from each. A variety of types of amino acid solutions were adopted to investigate the effects of pH and I in a manner that allows independent evaluation of each factor. The same effect could not be achieved using conventional buffer solutions. Size-exclusion chromatography, capillary differential scanning calorimetry, and fluorescence spectroscopy were utilized to probe the protein aggregation and conformation. The results suggested that, in addition to pH, solution ionic strength as a function of ionization state of the amino acid molecules and the ions introduced by pH adjustment played an important role in the aggregation and conformation of the protein studied. This experimental approach offers a useful tool to aid fundamental understanding of the relative effects of solution pH and ionic strength on protein stability.
%K Hydrogen-Ion Concentration, Osmolar Concentration, Protein Conformation, Recombinant Fusion Proteins, Solutions
%P 3065
%L 3074
%Y 10.1002/jps.24118
%W PHY
%G AUTHOR
%R 2014......103.3065Z

@Article{Zhou2014,
author="Zhou, Rong
and Nashine, Vishal
and Palm, Thomas
and Gandhi, Rajesh
and Adams, Monica",
title="Utilization of Zwitterion-based solutions to dissect the relative effects of solution pH and ionic strength on the aggregation behavior and conformational stability of a fusion protein.",
journal="Journal of pharmaceutical sciences",
year="2014",
month="Oct",
day="19",
volume="103",
number="10",
pages="3065--3074",
keywords="Hydrogen-Ion Concentration",
keywords="Osmolar Concentration",
keywords="Protein Conformation",
keywords="Recombinant Fusion Proteins",
keywords="Solutions",
abstract="Solution pH and ionic strength (I) have complex effects on protein stability. We developed an experimental approach based on exploitation of the zwitterionic characteristic of amino acid molecules to probe the relative contribution from each. A variety of types of amino acid solutions were adopted to investigate the effects of pH and I in a manner that allows independent evaluation of each factor. The same effect could not be achieved using conventional buffer solutions. Size-exclusion chromatography, capillary differential scanning calorimetry, and fluorescence spectroscopy were utilized to probe the protein aggregation and conformation. The results suggested that, in addition to pH, solution ionic strength as a function of ionization state of the amino acid molecules and the ions introduced by pH adjustment played an important role in the aggregation and conformation of the protein studied. This experimental approach offers a useful tool to aid fundamental understanding of the relative effects of solution pH and ionic strength on protein stability.",
issn="1520-6017",
doi="10.1002/jps.24118",
url="http://www.ncbi.nlm.nih.gov/pubmed/25139470",
language="eng"
}

%0 Journal Article
%T Utilization of Zwitterion-based solutions to dissect the relative effects of solution pH and ionic strength on the aggregation behavior and conformational stability of a fusion protein.
%A Zhou, Rong
%A Nashine, Vishal
%A Palm, Thomas
%A Gandhi, Rajesh
%A Adams, Monica
%J Journal of pharmaceutical sciences
%D 2014
%8 Oct 19
%V 103
%N 10
%@ 1520-6017
%G eng
%F Zhou2014
%X Solution pH and ionic strength (I) have complex effects on protein stability. We developed an experimental approach based on exploitation of the zwitterionic characteristic of amino acid molecules to probe the relative contribution from each. A variety of types of amino acid solutions were adopted to investigate the effects of pH and I in a manner that allows independent evaluation of each factor. The same effect could not be achieved using conventional buffer solutions. Size-exclusion chromatography, capillary differential scanning calorimetry, and fluorescence spectroscopy were utilized to probe the protein aggregation and conformation. The results suggested that, in addition to pH, solution ionic strength as a function of ionization state of the amino acid molecules and the ions introduced by pH adjustment played an important role in the aggregation and conformation of the protein studied. This experimental approach offers a useful tool to aid fundamental understanding of the relative effects of solution pH and ionic strength on protein stability.
%K Hydrogen-Ion Concentration
%K Osmolar Concentration
%K Protein Conformation
%K Recombinant Fusion Proteins
%K Solutions
%U http://dx.doi.org/10.1002/jps.24118
%U http://www.ncbi.nlm.nih.gov/pubmed/25139470
%P 3065-3074

PT Journal
AU Zhou, R
   Nashine, V
   Palm, T
   Gandhi, R
   Adams, M
TI Utilization of Zwitterion-based solutions to dissect the relative effects of solution pH and ionic strength on the aggregation behavior and conformational stability of a fusion protein.
SO Journal of pharmaceutical sciences
JI J Pharm Sci
PD Oct
PY 2014
BP 3065
EP 3074
VL 103
IS 10
DI 10.1002/jps.24118
LA eng
DE Hydrogen-Ion Concentration; Osmolar Concentration; Protein Conformation; Recombinant Fusion Proteins; Solutions
AB Solution pH and ionic strength (I) have complex effects on protein stability. We developed an experimental approach based on exploitation of the zwitterionic characteristic of amino acid molecules to probe the relative contribution from each. A variety of types of amino acid solutions were adopted to investigate the effects of pH and I in a manner that allows independent evaluation of each factor. The same effect could not be achieved using conventional buffer solutions. Size-exclusion chromatography, capillary differential scanning calorimetry, and fluorescence spectroscopy were utilized to probe the protein aggregation and conformation. The results suggested that, in addition to pH, solution ionic strength as a function of ionization state of the amino acid molecules and the ions introduced by pH adjustment played an important role in the aggregation and conformation of the protein studied. This experimental approach offers a useful tool to aid fundamental understanding of the relative effects of solution pH and ionic strength on protein stability.
ER

PMID- 25139470
OWN - NLM
STAT- MEDLINE
DA  - 20140925
DCOM- 20150601
IS  - 1520-6017 (Electronic)
IS  - 0022-3549 (Linking)
VI  - 103
IP  - 10
DP  - 2014 Oct
TI  - Utilization of Zwitterion-based solutions to dissect the relative effects of
      solution pH and ionic strength on the aggregation behavior and conformational
      stability of a fusion protein.
PG  - 3065-74
LID - 10.1002/jps.24118 [doi]
AB  - Solution pH and ionic strength (I) have complex effects on protein stability. We 
      developed an experimental approach based on exploitation of the zwitterionic
      characteristic of amino acid molecules to probe the relative contribution from
      each. A variety of types of amino acid solutions were adopted to investigate the 
      effects of pH and I in a manner that allows independent evaluation of each
      factor. The same effect could not be achieved using conventional buffer
      solutions. Size-exclusion chromatography, capillary differential scanning
      calorimetry, and fluorescence spectroscopy were utilized to probe the protein
      aggregation and conformation. The results suggested that, in addition to pH,
      solution ionic strength as a function of ionization state of the amino acid
      molecules and the ions introduced by pH adjustment played an important role in
      the aggregation and conformation of the protein studied. This experimental
      approach offers a useful tool to aid fundamental understanding of the relative
      effects of solution pH and ionic strength on protein stability.
CI  - (c) 2014 Wiley Periodicals, Inc. and the American Pharmacists Association.
FAU - Zhou, Rong
AU  - Zhou R
AD  - Drug Product Science & Technology, Bristol-Myers Squibb, New Brunswick, New
      Jersey, 08903.
FAU - Nashine, Vishal
AU  - Nashine V
FAU - Palm, Thomas
AU  - Palm T
FAU - Gandhi, Rajesh
AU  - Gandhi R
FAU - Adams, Monica
AU  - Adams M
LA  - eng
PT  - Journal Article
DEP - 20140819
PL  - United States
TA  - J Pharm Sci
JT  - Journal of pharmaceutical sciences
JID - 2985195R
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Solutions)
SB  - IM
MH  - *Hydrogen-Ion Concentration
MH  - *Osmolar Concentration
MH  - Protein Conformation
MH  - Recombinant Fusion Proteins/*chemistry
MH  - Solutions
OTO - NOTNLM
OT  - calorimetry (DSC)
OT  - chromatography
OT  - fluorescence spectroscopy
OT  - ionic strength
OT  - pH
OT  - protein aggregation
OT  - protein structure
OT  - zwitterion
EDAT- 2014/08/21 06:00
MHDA- 2015/06/02 06:00
CRDT- 2014/08/21 06:00
PHST- 2014/03/20 [received]
PHST- 2014/07/07 [revised]
PHST- 2014/07/23 [accepted]
PHST- 2014/08/19 [aheadofprint]
AID - 10.1002/jps.24118 [doi]
AID - S0022-3549(15)30375-0 [pii]
PST - ppublish
SO  - J Pharm Sci. 2014 Oct;103(10):3065-74. doi: 10.1002/jps.24118. Epub 2014 Aug 19.
TY  - JOUR
AU  - Zhou, Rong
AU  - Nashine, Vishal
AU  - Palm, Thomas
AU  - Gandhi, Rajesh
AU  - Adams, Monica
PY  - 2014/Oct/19
TI  - Utilization of Zwitterion-based solutions to dissect the relative effects of solution pH and ionic strength on the aggregation behavior and conformational stability of a fusion protein.
T2  - J Pharm Sci
JO  - Journal of pharmaceutical sciences
SP  - 3065
EP  - 3074
VL  - 103
IS  - 10
KW  - Hydrogen-Ion Concentration
KW  - Osmolar Concentration
KW  - Protein Conformation
KW  - Recombinant Fusion Proteins
KW  - Solutions
N2  - Solution pH and ionic strength (I) have complex effects on protein stability. We developed an experimental approach based on exploitation of the zwitterionic characteristic of amino acid molecules to probe the relative contribution from each. A variety of types of amino acid solutions were adopted to investigate the effects of pH and I in a manner that allows independent evaluation of each factor. The same effect could not be achieved using conventional buffer solutions. Size-exclusion chromatography, capillary differential scanning calorimetry, and fluorescence spectroscopy were utilized to probe the protein aggregation and conformation. The results suggested that, in addition to pH, solution ionic strength as a function of ionization state of the amino acid molecules and the ions introduced by pH adjustment played an important role in the aggregation and conformation of the protein studied. This experimental approach offers a useful tool to aid fundamental understanding of the relative effects of solution pH and ionic strength on protein stability.
SN  - 1520-6017
UR  - http://dx.doi.org/10.1002/jps.24118
UR  - http://www.ncbi.nlm.nih.gov/pubmed/25139470
ID  - Zhou2014
ER  - 
<?xml version="1.0" encoding="UTF-8"?>
<b:Sources SelectedStyle="" xmlns:b="http://schemas.openxmlformats.org/officeDocument/2006/bibliography"  xmlns="http://schemas.openxmlformats.org/officeDocument/2006/bibliography" >
<b:Source>
<b:Tag>Zhou2014</b:Tag>
<b:SourceType>ArticleInAPeriodical</b:SourceType>
<b:Year>2014</b:Year>
<b:Month>Oct</b:Month>
<b:Day>19</b:Day>
<b:PeriodicalName>Journal of pharmaceutical sciences</b:PeriodicalName>
<b:Volume>103</b:Volume>
<b:Issue>10</b:Issue>
<b:Pages>3065-3074</b:Pages>
<b:Author>
<b:Author><b:NameList>
<b:Person><b:Last>Zhou</b:Last><b:First>Rong</b:First></b:Person>
<b:Person><b:Last>Nashine</b:Last><b:First>Vishal</b:First></b:Person>
<b:Person><b:Last>Palm</b:Last><b:First>Thomas</b:First></b:Person>
<b:Person><b:Last>Gandhi</b:Last><b:First>Rajesh</b:First></b:Person>
<b:Person><b:Last>Adams</b:Last><b:First>Monica</b:First></b:Person>
</b:NameList></b:Author>
</b:Author>
<b:Title>Utilization of Zwitterion-based solutions to dissect the relative effects of solution pH and ionic strength on the aggregation behavior and conformational stability of a fusion protein.</b:Title>
 <b:ShortTitle>J Pharm Sci</b:ShortTitle>
<b:Comments>Solution pH and ionic strength (I) have complex effects on protein stability. We developed an experimental approach based on exploitation of the zwitterionic characteristic of amino acid molecules to probe the relative contribution from each. A variety of types of amino acid solutions were adopted to investigate the effects of pH and I in a manner that allows independent evaluation of each factor. The same effect could not be achieved using conventional buffer solutions. Size-exclusion chromatography, capillary differential scanning calorimetry, and fluorescence spectroscopy were utilized to probe the protein aggregation and conformation. The results suggested that, in addition to pH, solution ionic strength as a function of ionization state of the amino acid molecules and the ions introduced by pH adjustment played an important role in the aggregation and conformation of the protein studied. This experimental approach offers a useful tool to aid fundamental understanding of the relative effects of solution pH and ionic strength on protein stability.</b:Comments>
</b:Source>
</b:Sources>