Spectroscopic assessment of sinusoidal mechanical vibration exposed lyophilized human haemoglobin A
Year: 2025
Type: article
Abstract: Mechanical vibration plays a major role in protein folding and its function. Many degenerative diseases are caused by misfolding of proteins. Haemorheology, and haemodynamic depends on the oxygen transport mechanism of haemoglobin which is important in cardiovascular diseases and blood transfusion. Mechanical vibration during storage, transport, and shipping may affect the haemoglobin function. The main purpose of present work is to emphasis the effect of sinusoidal mechanical vibrations (SMV) on lyophilized haemoglobin powder. Lyophilized haemoglobin powder was treated with sinusoidal mechanical vibration at different frequencies ranging from 10, 20, 30, 40, and 50 Hz with an amplitude of 10 mm displacement for a 10-minute exposure time using an electrodynamic shaker. Conformational changes were estimated from UV–visible spectroscopy, FTIR spectroscopy, and Interfacial tension measurement (IFT) technique. Variation in absorbance was observed with no spectral shift at the Hb group position. The second derivative of FTIR spectra showed the difference in amide I-II band region between control and exposed haemoglobin. However, sinusoidal mechanical vibration also affects IFT at high frequencies i.e. 40 Hz and 50 Hz. The secondary structure of haemoglobin is influenced by sinusoidal mechanical vibration, which results in folding and a change in interfacial tension. Sinusoidal mechanical vibration (SMV) revealed haemoglobin alterations, indicating the need for improved handling or transportation procedures. Mechanical vibrations influence the stability of lyophilized powders by affecting their structural integrity. Understanding and controlling the effect of mechanical vibrations on lyophilized protein powder is essential in these applications to ensure the quality, efficacy, and safety of the final product.
Source: Next Materials
Authors: Sarika Hinge, Vijay Ghodake, Gauri Kulkarni
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $1,280
OpenAlex ID: W4411085577
