At HTL
Biosolutions, Inc., we offer both consulting and contract research
services on protein characterizations, stability testings and formulation development.
Raman spectroscopy has been
often used to investigate protein secondary structures
and side chain conformations. One of the major
advantages of Raman spectroscopy is its versatility to
study proteins in virtually all physical states,
including solution, solid, colloid and gel states.
ROA stands for Raman Optical
Activity and provides structural information about the
chiral property of a functional group.
Key Benefits of ROA
- Comparability study of
lot-to-lot variation
- Analysis of protein
tertiary structure
- Analysis of side chain
conformations, such as Trp, Tyr, S-S etc.
-
Raman and ROA spectra of
monoclonal antibody at pH 3 and 7.
Capabilities
- To
probe conformational changes in proteins
- ROA
can be used to detect changes in protein tertiary
and secondary structures. Protein side chain
conformations including Trp, Tyr and Cys can also
be determined by Raman and ROA spectroscopy.
- To
distinguish different types of protein secondary
structures
- VCD
spectroscopy can be used to detect different types
of protein secondary structures including
alpha-helix, 310 helix, hydrated
alpha-helix, parallel and anti-parallel
beta-sheets.
- To
determine protein-protein and protein-ligand
interactions
- FTIR,
VCD, Raman and ROA can be used to probe structural
changes in proteins resulted from protein-protein
and/or protein-ligand interactions.
Key
Benefits of Raman Spectroscopy
- Comparability
study of lot-to-lot variations
- Analysis
of protein secondary structures and side chain
conformations
- Analysis
of DNA and RNA conformations
- Ananlysis
of protein-DNA and protein-RNA interactions
- Analysis
of virus structures and assembly-disassembly
process of viruses
Capabilities
- Analysis of solid
protein samples
- Raman spectroscopy can be
used as an effective tool to study structure of
proteins in solid states, such as lyophilized
protein formulations, spray-dried protein powders,
and that of proteins in sustained release
formulations such as PLGA microspheres or other
solid dosage forms.
-
- Analysis of
protein-excipient interactions
- Effect of formulation
excipients such as sugars, polymers and
preservatives on protein structure can be studied
by using Raman spectroscopy.
-
- Analysis of
protein degradants
- Structures of protein
degradants such as oxidized protein, fragments and
deamindated proteins can be studied by using Raman
spectroscopy.
References
1.
Li, T.,
Chen, Z., Johnson, J.E. and Thomas, G.J., Jr.,
Conformations, Interactions, and Thermostabilities of
RNA and Proteins in Bean Pod Mottle Virus:
Investigation of Solution and Crystal Structures by
Laser Raman Spectroscopy, Biochemistry, 31,
6673-6682 (1992).
2.
Li, T., Bamford,
J.K.H., Bamford, D.H. and Thomas, G.J., Jr.,
Structural Studies of the Eveloped dsRNA Bacteriophage
ø6 of Pseudomonas syringae by Raman Spectroscopy.
I. The Virion and Its
Membrane, J. Mol. Biol., 230,
461-472 (1993).
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