Jyotsana Pathak

• PhD
• PostDoc Position at Indian Institute of Science Education and Research, Bhopal

In this review, a number of systems are described to demonstrate the effect of polyelectrolyte chain stiffness (persistence length) on the coacervation phenomena, after we briefly review the field. We consider two specific types of complexation/coacervation: in the first type, DNA is used as a fixed substrate binding to flexible polyions such as ge...

Herein, we report the comparative study of gels and complex coacervates of Bovine Serum Albumin (BSA) and beta-lactoglobulin (β-Lg) and gelatin near to their common pI. Surface patch binding produced variable new soft matter phases (intermolecular complexes) such as opaque coacervates (phase-I, charge neutralized) and transparent gels (phase-II, ov...

We have investigated the gelation behavior of polyampholyte gelatin B (GB) in the presence of colloidal plasma protein bovine serum albumin (BSA) as a function of mixing ratio (r = GB:BSA = 1.5, 2, 3, 4), pH (acidic, basic and neutral), and temperature (20–45 °C). Both the bio-molecules have identical isoelectric pH, and similar zeta potential prof...

An understanding of the interactions between gelatin B (GB) and β-lacto-globulin (β-Lg) mainly arising from surface selective patch binding occurring at their common pI (≈5.0 ± 0.5) in the absence of added salt. Heterogeneous surface charge distribution on β-Lg facilitated such interaction at different mixing ratio ([GB]: [β-Lg] = r) and the GB–β-L...

The interactions between water-soluble semiconductor quantum dots [hydrophilic 3-mercaptopropionic acid (MPA)-coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β-lactoglobulin (β-Lg) and human serum albumin (HSA), are investigated. Acidic residues of protein molecules form electrostatic interactions with these qua...

In this work, we report exclusive separation of Bovine Serum Albumin (BSA) from a solution where this protein was present with β-lactoglobulin (β-Lg) in 1:0.75 (w/v) ratio at their common isoelectric pH (5±0.02). A polyampholytic polypeptide Gelatin B (GB) also having the same pI was used to extract protein (BSA or β-Lg) molecules selectively from...

Herein, we report interaction between Bovine Serum Albumin ([BSA] = 1% (w/v)) and gelatin B ([GB] = 0.25-3.5 % (w/v)) occurring close to their common isoelectric pH (pI). This interaction generated distinguishable multiple soft matter phases like opaque coacervates (phase-I) and transparent gels (phase-II), where the former comprised of partially c...

Surface selective patch binding (SPB) interaction occurring between two protein molecules, bovine serum albumin (BSA) and gelatin B (GB), both having same isoelectric pH (pI ≈ 5) and identical pH-zeta potential profile, was systematically examined. BSA : GB mixing ratio r was varied in the range 0.16–2.00 and ionic strength was varied in the range...

Water-soluble luminescent colloidal quantum dots (QDs) have attracted much attention in biological and medical applications as drug carriers and imaging agents for cells. Investigations of protein–nanoparticle interaction play a key role in biomedical application because when nanoparticles enter the cellular environment, they strongly interact with...

We present a systematic investigation of the effect of solvent hydrophobicity (alkyl chain length) on the gelation kinetics and the phase states of the polypeptide gelatin in imidazolium based ionic liquid (IL) solutions. We have observed that IL concentration and hydrophobicity had dramatic influences on the thermal and viscoelastic properties of...

The effect of persistence length on the intermolecular binding of DNA (200 bp, persistence length lp = 50 nm, polyanion) with three proteins, gelatin B (GB) (lp = 2 nm, polyampholyte chain), bovine serum albumin (BSA) (lp = 7 nm, polyampholyte colloid), gelatin A (GA) (lp = 10 nm, polyampholyte chain), and a polysaccharide chitosan (lp = 17 nm, pol...