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<title>Department of Biophysics</title>
<link href="http://192.168.1.40:8080/xmlui/handle/123456789/8" rel="alternate"/>
<subtitle>D-BIO-PH</subtitle>
<id>http://192.168.1.40:8080/xmlui/handle/123456789/8</id>
<updated>2026-05-31T09:42:58Z</updated>
<dc:date>2026-05-31T09:42:58Z</dc:date>
<entry>
<title>Structural and Functional Studies of Designed Antimicrobial &amp; Anti-Inflammatory Peptides:</title>
<link href="http://192.168.1.40:8080/xmlui/handle/123456789/3527" rel="alternate"/>
<author>
<name>Ilyas, Humaira</name>
</author>
<id>http://192.168.1.40:8080/xmlui/handle/123456789/3527</id>
<updated>2021-07-22T10:38:20Z</updated>
<published>2020-01-01T00:00:00Z</published>
<summary type="text">Structural and Functional Studies of Designed Antimicrobial &amp; Anti-Inflammatory Peptides:
Ilyas, Humaira
Multi-drug resistant (MDR) bacteria or superbugs have become a global threat to human life due to their inherent&#13;
resistance to antibiotics. In this context, antimicrobial peptides (AMPs) have emerged as promising alternatives&#13;
owing to their unique structural and functional characteristics. In fact, AMPs are less susceptible to bacterial&#13;
resistance than traditional antibiotics. Structural insights into these AMPs using NMR spectroscopy have shown&#13;
a large correlation between the structure and biological properties of different classes of AMPs, a fact utilised for&#13;
designing newer peptide-based antibiotics. Approaches aiming to improve the potency and stability of peptides&#13;
necessitate understanding the sequence-structure-function relationship in developing and designing AMP-based&#13;
drugs. In contrast to the significant progress over the last decade, particularly regarding AMP optimization,&#13;
delivery aspects of AMPs have been less addressed, despite the potential of delivery systems to improve AMP&#13;
performance.&#13;
This works aims to (i) Characterize, study, and overcome the limitations associated with peptide-based therapy&#13;
using the technique of de novo antimicrobial peptide designing, which are effective against plant and animal&#13;
disease-causing pathogens. The structural insights of AMPs interacting with bacterial membrane components will&#13;
also pave the way to develop novel antimicrobial biopeptides. Initial investigation of the LK series of peptides led&#13;
to the designing of short AMPs that would economize the cost and time of synthesis associated with the largescale&#13;
synthesis of AMPs to be used as therapeutic molecules. Of the five designed peptides, P2-P6, P4, and P5&#13;
were effective against bacterial strains belonging to the ESKAPE group as well as human fungal opportunistic&#13;
pathogens. Structural correlation revealed that secondary structures are not a prerequisite for functional attributes&#13;
in the case of short peptides. Additionally, the emphasis was made to understand the phenomenon of peptide&#13;
synergism by studying the enhanced potency of VG16KRKP and KYE28, 16- and 28-mer de novo designed&#13;
peptides, respectively, when used in conjunction with one other. NMR spectroscopy of the complex formed&#13;
between these two peptides and their mutated analogs led to discovering an unusual peptide complex,&#13;
characterized by the formation of a bulky hydrophobic hub, stabilized by aromatic zippers highlighting this&#13;
structure as key for elevating antimicrobial potency of the peptide combination. Furthermore, insights into the&#13;
activity of the anti-inflammatory peptide KYE28 and its PEGylated variants have been investigated to correlate&#13;
their ability to disintegrate LPS aggregates and the ability of PEGylation for reducing toxicity and proteolytic&#13;
susceptibility of AMPs. (ii) Additionally, it also involves probing and studying potential nano-materials as AMP&#13;
delivery systems such that AMPs can be used for treating systemic diseases. In this context, it is worth mentioning&#13;
that AMPs need to penetrate the cell to target the microbes. Various techniques have been developed for modifying&#13;
natural AMPs, making them better suited to cross the cell membrane and get explicitly delivered to the target&#13;
bacterial membrane. Gold nanoparticle conjugation and poly (ethylene glycol) conjugation are two such delivery&#13;
techniques studied in this work. NMR-based structural insights depicted that both the conjugation techniques&#13;
increase the peptides' bioavailability without hampering their functional attributes.
</summary>
<dc:date>2020-01-01T00:00:00Z</dc:date>
</entry>
<entry>
<title>Understanding Transcription Factor Specificity and Design of Synthetic Transcription Factor</title>
<link href="http://192.168.1.40:8080/xmlui/handle/123456789/3498" rel="alternate"/>
<author>
<name>Ghosh, Basusree, Auth</name>
</author>
<author>
<name>Roy, Siddhartha, Supervisor</name>
</author>
<id>http://192.168.1.40:8080/xmlui/handle/123456789/3498</id>
<updated>2019-07-23T08:29:04Z</updated>
<published>2018-01-01T00:00:00Z</published>
<summary type="text">Understanding Transcription Factor Specificity and Design of Synthetic Transcription Factor
Ghosh, Basusree, Auth; Roy, Siddhartha, Supervisor
Awarded from University of Calcutta
</summary>
<dc:date>2018-01-01T00:00:00Z</dc:date>
</entry>
<entry>
<title>Structural and biophysical aspects of G, C rich nucleic acids</title>
<link href="http://192.168.1.40:8080/xmlui/handle/123456789/3459" rel="alternate"/>
<author>
<name>Mondal, Soma, Auth</name>
</author>
<author>
<name>Chatterje, Subhrangsu, Supervisor</name>
</author>
<id>http://192.168.1.40:8080/xmlui/handle/123456789/3459</id>
<updated>2018-11-27T12:17:03Z</updated>
<published>2017-01-01T00:00:00Z</published>
<summary type="text">Structural and biophysical aspects of G, C rich nucleic acids
Mondal, Soma, Auth; Chatterje, Subhrangsu, Supervisor
Awarded from University of Calcutta
</summary>
<dc:date>2017-01-01T00:00:00Z</dc:date>
</entry>
<entry>
<title>Structural insights into de-novo designed antimicrobial peptides : mechanistic analysis against plant and animal pathogens</title>
<link href="http://192.168.1.40:8080/xmlui/handle/123456789/3393" rel="alternate"/>
<author>
<name>Datta, Aritreyee, Auth</name>
</author>
<author>
<name>Bhunia, Anirban, Supervisor</name>
</author>
<id>http://192.168.1.40:8080/xmlui/handle/123456789/3393</id>
<updated>2018-11-27T12:18:55Z</updated>
<published>2017-01-01T00:00:00Z</published>
<summary type="text">Structural insights into de-novo designed antimicrobial peptides : mechanistic analysis against plant and animal pathogens
Datta, Aritreyee, Auth; Bhunia, Anirban, Supervisor
awarded from University of Calcutta
</summary>
<dc:date>2017-01-01T00:00:00Z</dc:date>
</entry>
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