The second virial coefficient as a predictor of protein aggregation propensity: A self-interaction chromatography study.
作者： A. Quigley , D.R. Williams
DOI: 10.1016/J.EJPB.2015.07.025
关键词:
摘要: The second osmotic virial coefficients (b2) of four proteins – lysozyme, recombinant human lactoferrin, concanavalin A and catalase were measured by self-interaction chromatography (SIC) in solutions varying salt type, concentration pH. Protein aggregate sizes based on the initial hydrodynamic radius protein solution species present using dynamic light scattering, relationship between b2 size was studied. linear correlation established values for all proteins, almost conditions. Aggregate 0. observed trends as a function conditions very much dependent, with notable including existence attractive interactions (negative values) at low ionic strengths A, highly positive lactoferrin over wide range conditions, reflecting lactoferrin’s innately high stability. It is concluded that quantification protein–protein SIC data potentially valuable screening tool predicting aggregation propensity.
core.ac.uk
imperial.ac.uk
sci-hub.se 参考文章(62)
Y. U. Moon, R. A. Curtis, C. O. Anderson, H. W. Blanch, J. M. Prausnitz, Protein-protein interactions in aqueous ammonium sulfate solutions. Lysozyme and bovine serum albumin (BSA) Journal of Solution Chemistry. ,vol. 29, pp. 699- 718 ,(2000) , 10.1023/A:1005112927213
A. George, Y. Chiang, B. Guo, A. Arabshahi, Z. Cai, W.William Wilson, [6] Second virial coefficient as predictor in protein crystal growth. Methods in Enzymology. ,vol. 276, pp. 100- 110 ,(1997) , 10.1016/S0076-6879(97)76052-X
John R. Conder, Colin Leslie Young, Physicochemical measurement by gas chromatography Wiley. ,(1979)
M M Ries-Kautt, A F Ducruix, Relative effectiveness of various ions on the solubility and crystal growth of lysozyme. Journal of Biological Chemistry. ,vol. 264, pp. 745- 748 ,(1989) , 10.1016/S0021-9258(19)85005-6
Eva Y. Chi, Sampathkumar Krishnan, Theodore W. Randolph, John F. Carpenter, Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation Pharmaceutical Research. ,vol. 20, pp. 1325- 1336 ,(2003) , 10.1023/A:1025771421906
Patrick H. C. van BERKEL, Harry A. van VEEN, Marlieke E. J. GEERTS, Herman A. de BOER, Jan H. NUIJENS, Heterogeneity in utilization of N-glycosylation sites Asn624 and Asn138 in human lactoferrin: a study with glycosylation-site mutants. Biochemical Journal. ,vol. 319, pp. 117- 122 ,(1996) , 10.1042/BJ3190117
Fangyu Hu, Fenggang Pan, Yoriko Sawano, Tsukasa Makino, Yuji Kakehi, Makoto Komiyama, Hiroshi Kawakami, Masaru Tanokura, Studies of the structure of multiferric ion-bound lactoferrin: A new antianemic edible material International Dairy Journal. ,vol. 18, pp. 1051- 1056 ,(2008) , 10.1016/J.IDAIRYJ.2008.05.003
Ashoka Sreedhara, Ragnar Flengsrud, Vishweshwaraiah Prakash, Daniel Krowarsch, Thor Langsrud, Purnima Kaul, Tove G. Devold, Gerd E. Vegarud, A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin. International Dairy Journal. ,vol. 20, pp. 487- 494 ,(2010) , 10.1016/J.IDAIRYJ.2010.02.003
Christopher J. Roberts, Tapan K. Das, Erinc Sahin, Predicting solution aggregation rates for therapeutic proteins: approaches and challenges. International Journal of Pharmaceutics. ,vol. 418, pp. 318- 333 ,(2011) , 10.1016/J.IJPHARM.2011.03.064
Danny K. Chou, Rajesh Krishnamurthy, Mark Cornell Manning, Theodore W. Randolph, John F. Carpenter, Physical stability of albinterferon-α(2b) in aqueous solution: effects of conformational stability and colloidal stability on aggregation. Journal of Pharmaceutical Sciences. ,vol. 101, pp. 2702- 2719 ,(2012) , 10.1002/JPS.23215