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Second Derivative Tryptophan Fluorescence Spectroscopy as a Tool to Characterize Partially Unfolded Intermediates of Proteins by Vineet Kumar; Vikas K. Sharma; Devendra S. Kalonia is a Pharmacology, Toxicology and Pharmaceutics article available to read on EtoBox.

What is Second Derivative Tryptophan Fluorescence Spectroscopy as a Tool to Characterize Partially Unfolded Intermediates of Proteins about?

The application of second derivative tryptophan (Trp) fluorescence spectroscopy to characterize partially unfolded intermediates of proteins relevant to protein formulation was investigated. The second derivatives of the normalized emission scans of N-acetyl tryptophanamide (NATA), single-Trp containing proteins, somatostatin and human serum albumin (HSA), and two-Trp containing proteins previously shown to form partially unfolded intermediates, beta-lactoglobulin (beta Lg) and interferon alpha-2a (IFN alpha 2a), were studied in solution. The second derivative of NATA in water showed three bands at 340, 348 and 367 nm. The 340 nm band showed a blue shift, whereas the intensity of all three bands was affected by a decrease in solution polarity. Second derivative of single-Trp containing proteins, somatostatin and HSA, showed three negative bands, whereas, the second derivative of the two-Trp containing proteins, beta Lg and IFN alpha 2a, showed four bands, two of which lie in the 320-340 nm range. These two bands were attributed to the presence of the Trps in different microenvironments. The characteristic changes in the intensities of these two bands on addition of guanidine hydroc

Who reads Second Derivative Tryptophan Fluorescence Spectroscopy as a Tool to Characterize Partially Unfolded Intermediates of Proteins?

Author

Vineet Kumar; Vikas K. Sharma; Devendra S. Kalonia

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0378-5173)

Published

2005

Language

EN

Field

Pharmacology, Toxicology and Pharmaceutics (Life Sciences)