تجاوز إلى المحتوى الرئيسي
User Image

Ajamaluddin Malik

أستاذ مشارك

Associate Professor

كلية العلوم
Building no 5, room no 2A46
المنشورات
مقال فى مجلة
2018

Unraveling the molecular mechanism of sodium dodecyl sulfate, salts, and sugars into amyloid fibril formation in camel IgG

Khan, Mohamad Alhasan Ismael, Javed Masood Khan, Ajamaluddin Malik, Rizwan Hasan . 2018

Sodium dodecyl sulfate (SDS) is an anionic surfactant that can be used to stimulate protein fibrillation in vitro. Here, we investigated the effects of SDS on camel IgG aggregation at pH 3.5 and 7.4. SDS-induced amyloid fibril formation in camel IgG was examined by turbidity measurements, Rayleigh scattering, Thioflavin T (ThT) fluorescence, intrinsic fluorescence, circular dichroism (CD), and transmission electron microscopy (TEM). The results suggest that low SDS concentrations (0.2-2.0 mM) induce amyloid-like aggregates of camel IgG at pH 3.5, indicating an SDS/camel IgG ratio below 1000. However, in the presence of higher concentrations of SDS (2.5-10.0 mM), amyloid fibril formation was not observed. Furthermore, at the higher concentrations, the β-sheet structure of camel IgG was transformed into a α-helical structure. The amyloid fibril formation was not observed in the presence of SDS at pH 7.4. Additionally, the role of salts and sugars was evaluated in the SDS-induced aggregation process. Interestingly, in the presence of 0.15 N of NaCl and (NH4)2SO4, SDS promoted camel IgG aggregation up to very high concentrations of SDS (0.2-10.0 mM; SDS/camel IgG ratio, 95-4750) and no suppression was observed. Moreover, osmoprotectants (trehalose and sucrose) were ineffective, neither promoting nor inhibiting the SDS-induced aggregation process. However, at pH 3.5, electrostatic and hydrophobic interactions, and hydrogen bonds were the major contributing factors in SDS-induced fibrillation. However, no aggregation was observed at pH 7.4 due to electrostatic repulsion between SDS and camel IgG because both of these molecules have overall similar charges.

رقم المجلد
170
مجلة/صحيفة
Colloids Surf B Biointerfaces.
الصفحات
430-437.
مزيد من المنشورات
publications

This study investigates the interaction between Coomassie Brilliant Blue (CBB) dye and Hen Egg White Lysozyme (HEWL) through a combination of molecular docking, molecular dynamics (MD) simulations…

بواسطة MD Harun Rashid, Rohit Karn, Arnold Emerson, Javed Masood Khan, Ajamaluddin Malik, Abha Jain, Priyankar Sen
2025
تم النشر فى:
International Journal of Biological Macromolecules
publications

Sodium lauroyl sarcosinate (SLS), an anionic surfactant is known to solubilize recombinant proteins during purification processes. Though SLS has been shown to induce amyloid fibrillation in…

بواسطة Ajamaluddin Malik, Javed Masood Khan, Md Tabish Rehman, Abdulaziz Alamri, Mohammad Amir, Prerna Sharma, Mohamed FAlAjmi, Sadaf Fatima
2025
تم النشر فى:
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
publications

This study investigates the aggregation behavior of human serum albumin (HSA) in its cationic (pH 2.0) and anionic (pH 8.0) states upon exposure to hexametaphosphate (HMP), a polyanionic compound…

بواسطة Nasser Abdulatif Al‐Shabib, Javed Masood Khan, Ajamaluddin Malik, Abdulaziz Alamri, Abdullah S Alhomida, Fohad Mabood Husain
2025
تم النشر فى:
JOURNAL OF MOLECULAR RECOGNITION