UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics

Oladepo, Sulayman A.; Xiong, Kan; Hong, Zhenmin; Asher, Sanford A.; Handen, Joseph; Lednev, Igor K.

doi:10.1021/cr200198a

Cited by 181 publications

(205 citation statements)

References 170 publications

(459 reference statements)

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“…176 In 2012, the utility of UVRRS as a tool for fast biopharmaceutical characterization of proteins was investigated and the secondary structure of the salmon calcitonin (sCT) protein was probed. Protein solutions of different concentrations were investigated (0.5-200 mg/mL) Figure 11.…”

Section: Analysis Of Biopharmaceutical Productsmentioning

confidence: 99%

Applications of Raman Spectroscopy in Biopharmaceutical Manufacturing: A Short Review

2017

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The production of active pharmaceutical ingredients (APIs) is currently undergoing its biggest transformation in a century. The changes are based on the rapid and dramatic introduction of protein-and macromolecule-based drugs (collectively known as biopharmaceuticals) and can be traced back to the huge investment in biomedical science (in particular in genomics and proteomics) that has been ongoing since the 1970s. Biopharmaceuticals (or biologics) are manufactured using biological-expression systems (such as mammalian, bacterial, insect cells, etc.) and have spawned a large (>E35 billion sales annually in Europe) and growing biopharmaceutical industry (BioPharma). The structural and chemical complexity of biologics, combined with the intricacy of cell-based manufacturing, imposes a huge analytical burden to correctly characterize and quantify both processes (upstream) and products (downstream). In small molecule manufacturing, advances in analytical and computational methods have been extensively exploited to generate process analytical technologies (PAT) that are now used for routine process control, leading to more efficient processes and safer medicines. In the analytical domain, biologic manufacturing is considerably behind and there is both a huge scope and need to produce relevant PAT tools with which to better control processes, and better characterize product macromolecules. Raman spectroscopy, a vibrational spectroscopy with a number of useful properties (nondestructive, non-contact, robustness) has significant potential advantages in BioPharma. Key among them are intrinsically high molecular specificity, the ability to measure in water, the requirement for minimal (or no) sample pre-treatment, the flexibility of sampling configurations, and suitability for automation. Here, we review and discuss a representative selection of the more important Raman applications in BioPharma (with particular emphasis on mammalian cell culture). The review shows that the properties of Raman have been successfully exploited to deliver unique and useful analytical solutions, particularly for online process monitoring. However, it also shows that its inherent susceptibility to fluorescence interference and the weakness of the Raman effect mean that it can never be a panacea. In particular, Raman-based methods are intrinsically limited by the chemical complexity and wide analyte-concentration-profiles of cell culture media/bioprocessing broths which limit their use for quantitative analysis. Nevertheless, with appropriate foreknowledge of these limitations and good experimental design, robust analytical methods can be produced. In addition, new technological developments such as time-resolved detectors, advanced lasers, and plasmonics offer potential of new Raman-based methods to resolve existing limitations and/or provide new analytical insights.

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Section: Analysis Of Biopharmaceutical Productsmentioning

confidence: 99%

Applications of Raman Spectroscopy in Biopharmaceutical Manufacturing: A Short Review

2017

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“…Therefore, we characterized the structure of the isoforms by DUVRR spectroscopy, a powerful tool for structural characterization of proteins in both refolded and misfolded oligomeric forms (17,18). A high sensitivity of DUVRR spectra to the protein secondary structure is based on the dependence of amide vibrational modes on and dihedral angles determining the three-dimensional conformation of the polypeptide backbone (17,18). DUVRR spectra are most sensitive to ␤-sheet and unordered protein conformations in contrast to CD, which is most sensitive to ␣-helix.…”

Section: Saa11 Is Less Stable Than Saa22 Despite Similar Secondary mentioning

confidence: 99%

“…Amide II and amide III bands involve significant C-N stretching, N-H bending, and C-C stretching. The C ␣ -H bending vibration mode involves C ␣ -H symmetric bending and C-C ␣ stretching (17).…”

Section: Saa11 Is Less Stable Than Saa22 Despite Similar Secondary mentioning

confidence: 99%

Pathogenic Serum Amyloid A 1.1 Shows a Long Oligomer-rich Fibrillation Lag Phase Contrary to the Highly Amyloidogenic Non-pathogenic SAA2.2

Srinivasan

Patke

Wang

et al. 2013

Journal of Biological Chemistry

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Background: Murine SAA1.1 is pathogenic and SAA2.2 is non-pathogenic in AA amyloidosis. Results: SAA1.1 and SAA2.2 exhibit different biophysical properties, including fibrillation kinetics and fibril morphology. Conclusion:The distinct biophysical properties of highly homologous SAA proteins may contribute to their different pathogenicity during chronic inflammation. Significance: Structural and kinetic factors, more than their intrinsic amyloidogenicity, may determine the diverse pathogenicity among nearly identical SAA isoforms.

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“…19,20 Coupling of hydrogen-deuterium exchange (H/D exchange) with deep UV Raman (DUVRR) spectroscopy allows one to elucidate fibril core structural organization and determine the psi (Ψ) dihedral angle of the protein backbone. 18,[21][22][23] In addition, DUVRR provides valuable information about the local environment near aromatic amino acids, such as phenylalanine and tyrosine. This can be utilized to monitor the changes in protein secondary structure that occur upon protein aggregation.…”

Section: Introductionmentioning

confidence: 99%

Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

Kurouski

Duyne

Lednev

2015

Analyst

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Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and scanning electron (SEM) microscopies, Raman spectroscopy becomes a powerful spectroscopic approach that can investigate the structural organization of amyloid fibril polymorphs. In this review, we discuss the applications of Raman spectroscopy, a unique, label-free and non-destructive technique for the structural characterization of amyloidogenic proteins, prefibrilar oligomers, and mature fibrils.

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UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics

Cited by 181 publications

References 170 publications

Applications of Raman Spectroscopy in Biopharmaceutical Manufacturing: A Short Review

Applications of Raman Spectroscopy in Biopharmaceutical Manufacturing: A Short Review

Pathogenic Serum Amyloid A 1.1 Shows a Long Oligomer-rich Fibrillation Lag Phase Contrary to the Highly Amyloidogenic Non-pathogenic SAA2.2

Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

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