Fourier transform infrared studies of proteins using nonaqueous solvents. Effects of methanol and ethylene glycol on albumin and immunoglobulin G

Wasacz, F. M.; Olinger, Jill M.; Jakobsen, R. J.

doi:10.1021/bi00379a038

Cited by 73 publications

(52 citation statements)

References 9 publications

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“…It shows that the deviation in the average of each characteristic frequency is in the worst case Ϯ5 cm Ϫ1 . These positions are in very good agreement with those reported in the literature for IgG using different IR methods (ATR and transmission) and using different mathematical manipulations of the data, such as SD, CF, or Fourier self-deconvolution (7,10,(21)(22)(23).…”

Section: Structural Analysissupporting

confidence: 89%

“…This multiplicity between 1620 and 1640 cm Ϫ1 of "␤-peaks" has been frequently observed in ␤-sheetcontaining proteins and reflects differences in the hydrogen bonding strength, as well as differences in transition dipole coupling in different ␤-strands (12). The high-frequency "␤-component" may overlap with contributions from ␤-turns and unordered structures, and it is not univocally related to a particular absorption peak: in the literature the peaks observed between 1690 and 1660 cm Ϫ1 were assigned to either ␤-turns or ␤-sheet (7,10,21). Based on the spectra of proteins with very high ␤-sheet content, Byler and Susi (7,13) assign the peaks observed in the region 1680 -1670 cm Ϫ1 to the highfrequency component of the ␤-sheet structure and suggested that the sum of all the integrated areas of the "␤-peaks," as a fraction of the total amide I band area, is closely related to the total "␤-content" of a given protein.…”

Section: Figmentioning

confidence: 99%

“…The only remarkable difference is the appearance of an extra peak, partly overlapping the dominant peak, centered at 1631 cm Ϫ1 , when IgG is adsorbed on the hydrophobic ϩ copolymer surface. Wasacz et al (21) reported a shift of the strongest amide I peak from 1638 to 1629 cm Ϫ1 , leaving a weak shoulder near 1640 cm Ϫ1 when ␥-globulins were transferred from aqueous solution to ethylene glycol. This shift was interpreted as a change in the ␤-sheet structure; i.e., the ␤-sheet type of ␥-globulins exposed to ethylene glycol are different from those observed in aqueous solution.…”

Section: Table 2 Comparison Of the Peak Positions Obtained With The Smentioning

confidence: 99%

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ATR-FTIR Study of IgG Adsorbed on Different Silica Surfaces

Giacomelli

Bremer

Norde

1999

Journal of Colloid and Interface Science

143

108

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Section: Structural Analysissupporting

confidence: 89%

Section: Figmentioning

confidence: 99%

Section: Table 2 Comparison Of the Peak Positions Obtained With The Smentioning

confidence: 99%

See 1 more Smart Citation

ATR-FTIR Study of IgG Adsorbed on Different Silica Surfaces

Giacomelli

Bremer

Norde

1999

Journal of Colloid and Interface Science

143

108

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“…This is because although the FTIR bands in the amide I region directly correspond to these secondary structural elements (16,17), the line broadening in the spectra of lyophilized proteins, combined with strongly overlapping bands, make such quantitation in this region arduous (15,18). Another spectral region, the amide III band (1220-1330 cm-'), also reflects the secondary structure of proteins (19)(20)(21) and has been used to characterize structural changes qualitatively (22)(23)(24)(25)(26) and, in aqueous solution, even to quantify the individual secondary structure composition of proteins (19)(20)(21)27). …”

mentioning

confidence: 99%

Lyophilization-induced reversible changes in the secondary structure of proteins.

Griebenow

Klibanov

1995

Proc. Natl. Acad. Sci. U.S.A.

349

311

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Changes in the secondary structure of some dozen different proteins upon lyophilization of their aqueous solutions have been investigated by means of Fouriertransform infrared spectroscopy in the amide IHI band region. Dehydration markedly (but reversibly) alters the secondary structure of all the proteins studied, as revealed by both the quantitative analysis of the second derivative spectra and the Gaussian curve fitting of the original infrared spectra. Lyophilization substantially increases the ,8-sheet content and lowers the a-helix content of all proteins. In all but one case, proteins become more ordered upon lyophilization.Consider the common laboratory and bioindustrial process of lyophilization or freeze-drying of aqueous solutions of proteins. Suppose that this lyophilization is carried out such that no irreversible damage to the protein ensues-i.e., when the lyophilized protein is redissolved in water, it exhibits the same properties as prior to lyophilization. The question still remains whether the protein structure in the lyophilized form is native or whether the lyophilization has resulted in reversible protein denaturation. Apart from its biochemical interest, the answer has important biotechnological implications. For example, proteins that have been lyophilized (which is how research and pharmaceutical protein preparations are usually stored) undergo moisture-triggered aggregation (1). To understand the mechanism of this undesirable phenomenon and to develop rational strategies for its prevention, structural information on proteins in the solid-e.g., lyophilized-form is needed. In addition, lyophilized enzymes suspended in organic solvents have proven to be useful synthetic catalysts (2); enzyme structural data should help maximize their performance.The issue of protein conformation in the lyophilized form is controversial. For example, the results of Fourier-transform infrared (FTIR) spectroscopic investigations of hen egg-white lysozyme were interpreted to indicate that lysozyme structure in either aqueous solution or the lyophilized state is the same (3-6). This conclusion was supported by some hydrogen isotope-exchange studies (6, 7) but contradicted by others (8). Raman (9-11) and solid-state NMR (12) studies have suggested significant (reversible) structural changes occurring in lysozyme upon lyophilization. Likewise, recent hydrogen isotope-exchange/high-resolution NMR (13) and FTIR (14,15) investigations of various proteins strongly point to lyophilization-induced reversible denaturation.Recent advances, both instrumentational and conceptual, in FTIR spectroscopy make it a method of choice for examining the structure of solid proteins. This has been illustrated by the scholarly work of Prestrelski et al. (14,15), who have employed this methodology to quantify changes in the secondary structure of proteins caused by lyophilization. Using the second derivatives of the vibrational spectra of proteins in the amide I band region (1600-1720 cm-1), these authors have calculated so-call...

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“…ATR-FTIR has been shown to be useful for studying the secondary structure and other properties of proteins in a variety of environments (5)(6)(7)(8)(9)(10)(11)(12)(13)(14). Two ATR methods have been used for studying soluble proteins.…”

mentioning

confidence: 99%