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Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.

Abstract A high-throughput thermal-scanning method to rank-order formulation conditions for therapeutic proteins is described. Apparent transition temperatures for unfolding and aggregation of four different proteins are determined using the dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions. The results indicate that the ThT-based thermal scanning method offers several advantages over the previously described SYPRO Orange-based thermal scanning and allows rapid rank ordering of solution conditions relevant toward long-term storage of therapeutic molecules. The method is also amenable to high protein concentration and does not require sample dilution or extensive preparation. Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to the screening of mutants for their unfolding and aggregation propensities.
PMID
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Authors

Mayor MeshTerms
Keywords
Journal Title aaps pharmscitech
Publication Year Start
%A Nashine, Vishal C.; Kroetsch, Andrew M.; Sahin, Erinc; Zhou, Rong; Adams, Monica L.
%T Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.
%J AAPS PharmSciTech, vol. 14, no. 4, pp. 1360-1366
%D 12/2013
%V 14
%N 4
%M eng
%B A high-throughput thermal-scanning method to rank-order formulation conditions for therapeutic proteins is described. Apparent transition temperatures for unfolding and aggregation of four different proteins are determined using the dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions. The results indicate that the ThT-based thermal scanning method offers several advantages over the previously described SYPRO Orange-based thermal scanning and allows rapid rank ordering of solution conditions relevant toward long-term storage of therapeutic molecules. The method is also amenable to high protein concentration and does not require sample dilution or extensive preparation. Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to the screening of mutants for their unfolding and aggregation propensities.
%K Algorithms, Antibodies, Monoclonal, Buffers, Chemistry, Pharmaceutical, Chymotrypsinogen, High-Throughput Screening Assays, Peptides, Protein Conformation, Protein Structure, Secondary, Proteins, Real-Time Polymerase Chain Reaction, Solubility, Spectrometry, Fluorescence, Temperature, Thiazoles
%P 1360
%L 1366
%Y 10.1208/s12249-013-0026-2
%W PHY
%G AUTHOR
%R 2013.......14.1360N

@Article{Nashine2013,
author="Nashine, Vishal C.
and Kroetsch, Andrew M.
and Sahin, Erinc
and Zhou, Rong
and Adams, Monica L.",
title="Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.",
journal="AAPS PharmSciTech",
year="2013",
month="Dec",
day="04",
volume="14",
number="4",
pages="1360--1366",
keywords="Algorithms",
keywords="Antibodies, Monoclonal",
keywords="Buffers",
keywords="Chemistry, Pharmaceutical",
keywords="Chymotrypsinogen",
keywords="High-Throughput Screening Assays",
keywords="Peptides",
keywords="Protein Conformation",
keywords="Protein Structure, Secondary",
keywords="Proteins",
keywords="Real-Time Polymerase Chain Reaction",
keywords="Solubility",
keywords="Spectrometry, Fluorescence",
keywords="Temperature",
keywords="Thiazoles",
abstract="A high-throughput thermal-scanning method to rank-order formulation conditions for therapeutic proteins is described. Apparent transition temperatures for unfolding and aggregation of four different proteins are determined using the dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions. The results indicate that the ThT-based thermal scanning method offers several advantages over the previously described SYPRO Orange-based thermal scanning and allows rapid rank ordering of solution conditions relevant toward long-term storage of therapeutic molecules. The method is also amenable to high protein concentration and does not require sample dilution or extensive preparation. Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to the screening of mutants for their unfolding and aggregation propensities.",
issn="1530-9932",
doi="10.1208/s12249-013-0026-2",
url="http://www.ncbi.nlm.nih.gov/pubmed/24002823",
language="eng"
}

%0 Journal Article
%T Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.
%A Nashine, Vishal C.
%A Kroetsch, Andrew M.
%A Sahin, Erinc
%A Zhou, Rong
%A Adams, Monica L.
%J AAPS PharmSciTech
%D 2013
%8 Dec 04
%V 14
%N 4
%@ 1530-9932
%G eng
%F Nashine2013
%X A high-throughput thermal-scanning method to rank-order formulation conditions for therapeutic proteins is described. Apparent transition temperatures for unfolding and aggregation of four different proteins are determined using the dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions. The results indicate that the ThT-based thermal scanning method offers several advantages over the previously described SYPRO Orange-based thermal scanning and allows rapid rank ordering of solution conditions relevant toward long-term storage of therapeutic molecules. The method is also amenable to high protein concentration and does not require sample dilution or extensive preparation. Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to the screening of mutants for their unfolding and aggregation propensities.
%K Algorithms
%K Antibodies, Monoclonal
%K Buffers
%K Chemistry, Pharmaceutical
%K Chymotrypsinogen
%K High-Throughput Screening Assays
%K Peptides
%K Protein Conformation
%K Protein Structure, Secondary
%K Proteins
%K Real-Time Polymerase Chain Reaction
%K Solubility
%K Spectrometry, Fluorescence
%K Temperature
%K Thiazoles
%U http://dx.doi.org/10.1208/s12249-013-0026-2
%U http://www.ncbi.nlm.nih.gov/pubmed/24002823
%P 1360-1366

PT Journal
AU Nashine, VC
   Kroetsch, AM
   Sahin, E
   Zhou, R
   Adams, ML
TI Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.
SO AAPS PharmSciTech
PD Dec
PY 2013
BP 1360
EP 1366
VL 14
IS 4
DI 10.1208/s12249-013-0026-2
LA eng
DE Algorithms; Antibodies, Monoclonal; Buffers; Chemistry, Pharmaceutical; Chymotrypsinogen; High-Throughput Screening Assays; Peptides; Protein Conformation; Protein Structure, Secondary; Proteins; Real-Time Polymerase Chain Reaction; Solubility; Spectrometry, Fluorescence; Temperature; Thiazoles
AB A high-throughput thermal-scanning method to rank-order formulation conditions for therapeutic proteins is described. Apparent transition temperatures for unfolding and aggregation of four different proteins are determined using the dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions. The results indicate that the ThT-based thermal scanning method offers several advantages over the previously described SYPRO Orange-based thermal scanning and allows rapid rank ordering of solution conditions relevant toward long-term storage of therapeutic molecules. The method is also amenable to high protein concentration and does not require sample dilution or extensive preparation. Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to the screening of mutants for their unfolding and aggregation propensities.
ER

PMID- 24002823
OWN - NLM
STAT- MEDLINE
DA  - 20131126
DCOM- 20140711
LR  - 20150423
IS  - 1530-9932 (Electronic)
IS  - 1530-9932 (Linking)
VI  - 14
IP  - 4
DP  - 2013 Dec
TI  - Orthogonal high-throughput thermal scanning method for rank ordering protein
      formulations.
PG  - 1360-6
LID - 10.1208/s12249-013-0026-2 [doi]
AB  - A high-throughput thermal-scanning method to rank-order formulation conditions
      for therapeutic proteins is described. Apparent transition temperatures for
      unfolding and aggregation of four different proteins are determined using the
      dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions.
      The results indicate that the ThT-based thermal scanning method offers several
      advantages over the previously described SYPRO Orange-based thermal scanning and 
      allows rapid rank ordering of solution conditions relevant toward long-term
      storage of therapeutic molecules. The method is also amenable to high protein
      concentration and does not require sample dilution or extensive preparation.
      Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to
      the screening of mutants for their unfolding and aggregation propensities.
FAU - Nashine, Vishal C
AU  - Nashine VC
AD  - Drug Product Science and Technology, Bristol-Myers Squibb, 1 Squibb Drive, New
      Brunswick, New Jersey, 08903, USA, [email protected]
FAU - Kroetsch, Andrew M
AU  - Kroetsch AM
FAU - Sahin, Erinc
AU  - Sahin E
FAU - Zhou, Rong
AU  - Zhou R
FAU - Adams, Monica L
AU  - Adams ML
LA  - eng
PT  - Journal Article
DEP - 20130904
PL  - United States
TA  - AAPS PharmSciTech
JT  - AAPS PharmSciTech
JID - 100960111
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Buffers)
RN  - 0 (Peptides)
RN  - 0 (Proteins)
RN  - 0 (Thiazoles)
RN  - 2390-54-7 (thioflavin T)
RN  - 9035-75-0 (Chymotrypsinogen)
SB  - IM
MH  - Algorithms
MH  - Antibodies, Monoclonal/administration & dosage/chemistry
MH  - Buffers
MH  - Chemistry, Pharmaceutical/*methods
MH  - Chymotrypsinogen
MH  - High-Throughput Screening Assays/*methods
MH  - Peptides/administration & dosage/chemistry
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Proteins/*chemistry
MH  - Real-Time Polymerase Chain Reaction
MH  - Solubility
MH  - Spectrometry, Fluorescence
MH  - Temperature
MH  - Thiazoles
PMC - PMC3840783
OID - NLM: PMC3840783
EDAT- 2013/09/05 06:00
MHDA- 2014/07/12 06:00
CRDT- 2013/09/05 06:00
PHST- 2013/06/10 [received]
PHST- 2013/08/20 [accepted]
PHST- 2013/09/04 [aheadofprint]
AID - 10.1208/s12249-013-0026-2 [doi]
PST - ppublish
SO  - AAPS PharmSciTech. 2013 Dec;14(4):1360-6. doi: 10.1208/s12249-013-0026-2. Epub
      2013 Sep 4.
TY  - JOUR
AU  - Nashine, Vishal C.
AU  - Kroetsch, Andrew M.
AU  - Sahin, Erinc
AU  - Zhou, Rong
AU  - Adams, Monica L.
PY  - 2013/Dec/04
TI  - Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.
JO  - AAPS PharmSciTech
SP  - 1360
EP  - 1366
VL  - 14
IS  - 4
KW  - Algorithms
KW  - Antibodies, Monoclonal
KW  - Buffers
KW  - Chemistry, Pharmaceutical
KW  - Chymotrypsinogen
KW  - High-Throughput Screening Assays
KW  - Peptides
KW  - Protein Conformation
KW  - Protein Structure, Secondary
KW  - Proteins
KW  - Real-Time Polymerase Chain Reaction
KW  - Solubility
KW  - Spectrometry, Fluorescence
KW  - Temperature
KW  - Thiazoles
N2  - A high-throughput thermal-scanning method to rank-order formulation conditions for therapeutic proteins is described. Apparent transition temperatures for unfolding and aggregation of four different proteins are determined using the dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions. The results indicate that the ThT-based thermal scanning method offers several advantages over the previously described SYPRO Orange-based thermal scanning and allows rapid rank ordering of solution conditions relevant toward long-term storage of therapeutic molecules. The method is also amenable to high protein concentration and does not require sample dilution or extensive preparation. Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to the screening of mutants for their unfolding and aggregation propensities.
SN  - 1530-9932
UR  - http://dx.doi.org/10.1208/s12249-013-0026-2
UR  - http://www.ncbi.nlm.nih.gov/pubmed/24002823
ID  - Nashine2013
ER  - 
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