Analyzing the structure of kallikrein-related peptidases with microfluidic modulation spectroscopy

Sponsored Content by Sino Biological Inc.May 14 2024Reviewed by Maria Osipova Kallikrein-related peptidases are key markers in cancer regulation, bearing on processes crucial for the survival and spread of cancer cells. For this study, RedShift Bio’s Microfluidic Modulation Spectroscopy was used to accurately determine the secondary structural makeup of kallikrein proteins.

KLKs act as biomarkers and therapy targets in various cancers and can help advance targeted treatments.7–12 Despite structural similarities, KLKs take on different roles in pathophysiology, underscoring the need to comprehend their structural distinctions, which is key for effective drug design. Utilizing Visual Molecular Dynamics, MMS can provide a robust, efficient method for analyzing KLK protein conformational structures in a solution. The data enables comparisons to be made and demonstrates key insights into protein activity.13

Structural motifs were identified using the Gaussian curve fitting as depicted in the HOS fractional contribution bar chart. Leveraging the overlap area in the inverted and baseline-subtracted second derivative plot, the quantitative results exhibited assessed repeatability against the control sample as shown in Table 2.

Comparing KLK proteins to chymotrypsinogen KLK-1 demonstrates dual specificity, exhibiting characteristics of both trypsin and chymotrypsin. On the contrary, both KLK-3 and KLK-7 are predominantly chymotrypsin-like proteins.2 This inconsistency, in part, accounts for KLK-1's considerably higher activity in comparison to the other two KLKs.

Table 3. A quantitative analysis of repeatability of each individual measurement as well as the comparison between KLK protein and chymotrypsinogen . Source: RedShift Bio

Source: Healthcare Press (healthcarepress.net)

Microfluidic Modulation Spectroscopy

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