{"id":5175,"date":"2026-05-13T15:05:48","date_gmt":"2026-05-13T19:05:48","guid":{"rendered":"https:\/\/oge.mit.edu\/msrp\/?post_type=profiles&#038;p=5175"},"modified":"2026-08-11T17:37:31","modified_gmt":"2026-08-11T21:37:31","slug":"zanyah-shepherd-2","status":"publish","type":"profiles","link":"https:\/\/oge.mit.edu\/msrp\/profiles\/zanyah-shepherd-2\/","title":{"rendered":"Zanyah Shepherd"},"content":{"rendered":"<div class=\"wp-block-image\">\n<figure class=\"alignleft size-full is-resized\"><img loading=\"lazy\" decoding=\"async\" width=\"400\" height=\"599\" src=\"https:\/\/oge.mit.edu\/msrp\/wp-content\/uploads\/sites\/2\/2026\/05\/Shepherd-Zanyah.jpg\" alt=\"by Corban Swain\" class=\"wp-image-5637\" style=\"aspect-ratio:1;object-fit:cover;width:200px;height:auto\" srcset=\"https:\/\/oge.mit.edu\/msrp\/wp-content\/uploads\/sites\/2\/2026\/05\/Shepherd-Zanyah.jpg 400w, https:\/\/oge.mit.edu\/msrp\/wp-content\/uploads\/sites\/2\/2026\/05\/Shepherd-Zanyah-200x300.jpg 200w\" sizes=\"auto, (max-width: 400px) 100vw, 400px\" \/><\/figure>\n<\/div>\n\n\n<div class=\"wp-block-group\"><div class=\"wp-block-group__inner-container is-layout-constrained wp-block-group-is-layout-constrained\">\n<p class=\"wp-block-paragraph\"><strong>Claflin University<\/strong><br>Faculty Advisor: Prof. Oleta Johnson<br>Research Supervisors: Natalie Heitman,<br>Berenice Estrada Chavez<br>Department: Chemistry<\/p>\n<\/div><\/div>\n\n\n\n<div style=\"height:0px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h4 class=\"wp-block-heading\"><strong>Biography<\/strong><\/h4>\n\n\n\n<p class=\"wp-block-paragraph\">Zanyah Shepherd is a rising junior chemistry major at Claflin University. Born in<br>Southeast, DC, and raised in Temple Hills, MD, she was surrounded by family members<br>in the medical field, which sparked her appreciation for healthcare. After a computational<br>bioinformatics internship at Howard University focused on protein stability and its role in<br>diseases like cancer, Zanyah realized her impact could take a different path. Then, through the<br>Environmental Science Summer Program experience at Claflin University, she developed a<br>passion for using chemistry to solve health challenges. She now aspires to collaborate across<br>disciplines to develop innovative methods, tools, and discoveries that aid in the prevention<br>or cure of developmental diseases through small-molecule research targeting understudied<br>cancer-related proteins. Zanyah plans to achieve her goals by pursuing a Ph.D., expanding<br>her network, and seizing opportunities like her current internship at MIT. Beyond science, she<br>enjoys reading, exercising, and practicing yoga.<\/p>\n\n\n\n<p class=\"has-text-align-center wp-block-paragraph\"><br><strong>Developing A DnaJB6 Chaperone Probe Through G\/F1-Derived<br>Peptide Optimization<br>Zanyah Shepherd1, Natalie Heitman2, Berenice Estrada Chavez2, Zahmiria Johnson2,<br>Dr. Oleta Johnson2<\/strong><br>1School of Natural Science and Mathematics, Claflin University<br>2Department of Chemistry, Massachusetts Institute of Technology<\/p>\n\n\n\n<p class=\"has-text-align-center wp-block-paragraph\"><br>DnaJB6 is a chaperone protein that suppresses protein aggregation associated with<br>numerous diseases, but its regulation remains poorly characterized due to its highly disordered<br>nature. Nevertheless, it is known to act on clients such as Tau and Polyglutamine-expanded<br>huntingtin, which are associated with neurodegenerative diseases. Mutant forms of DnaJB6 can<br>impair its ability to suppress protein aggregation, contributing to disease progression. Notably,<br>mutations in the G\/F1 region cause a muscular disease called Limb-Girdle Muscular Dystrophy<br>Type D1 (LGMDD1). Previous studies show that DnaJB6 has an autoinhibition mechanism in<br>which the G\/F1 region lies across its canonical J-domain, preventing interaction with Hsp70, a<br>co-chaperone of DnaJB6. This study leverages that region\u2019s autoinhibitory properties to inform the<br>design of a high-affinity DnaJB6-specific probe. Accordingly, this work builds on a peptide probe<br>developed by the Johnson Lab that mimics the G\/F1 sequence and binds to the J-domain with 90<br>uM affinity. To make this probe more experimentally tractable, we synthesized peptides<br>containing substitutions at the LGMDD1-associated residue F91 that were computationally<br>predicted to improve binding affinity. Ultimately, this optimization will enable the probe to be<br>applied to critical investigations of DnaJB6 function and regulation, yielding valuable insights into<br>its critical roles in proteostasis.<\/p>\n","protected":false},"featured_media":5420,"template":"","profile_category":[25],"class_list":["post-5175","profiles","type-profiles","status-publish","has-post-thumbnail","hentry","profile_category-2026-interns"],"acf":[],"_links":{"self":[{"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/profiles\/5175","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/profiles"}],"about":[{"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/types\/profiles"}],"version-history":[{"count":3,"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/profiles\/5175\/revisions"}],"predecessor-version":[{"id":5762,"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/profiles\/5175\/revisions\/5762"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/media\/5420"}],"wp:attachment":[{"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/media?parent=5175"}],"wp:term":[{"taxonomy":"profile_category","embeddable":true,"href":"https:\/\/oge.mit.edu\/msrp\/wp-json\/wp\/v2\/profile_category?post=5175"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}