Campus Access Only

All rights reserved. This publication is intended for use solely by faculty, students, and staff of University of the Pacific. No part of this publication may be reproduced, distributed, or transmitted in any form or by any means, now known or later developed, including but not limited to photocopying, recording, or other electronic or mechanical methods, without the prior written permission of the author or the publisher.

Date of Award


Document Type

Thesis - Pacific Access Restricted

Degree Name

Master of Science (M.S.)


Biological Sciences

First Advisor

Craig Vierra

First Committee Member

Geoffrey Lin-Cereghino

Second Committee Member

Lisa Wrischnik


The outstanding material properties of spider dragline silk fibers have been attributed to two spidroins, MaSp1 and MaSp2. Although dragline silk fibers have been treated with different chemical solvents to elucidate the relationship between protein structure and fiber mechanics, there has not been a comprehensive proteomic analysis of the major ampullate (MA) gland, its spinning dope, and dragline silk using a wide range of chaotropic agents, inorganic salts, and fluorinated alcohols to elucidate their complete molecular constituents. In these studies, we perform in-solution tryptic digestions of solubilized MA glands, spinning dope and dragline silk fibers using 5 different solvents, followed by nanoLC-MS/MS analysis with an Orbitrap Fusion™ Tribrid™ mass spectrometer. To improve protein identification, we employed three different tryptic peptide fragmentation modes, which included CID, HCD, and ETD to discover proteins involved in the silk assembly pathway and silk fiber. In addition to MaSp1 and MaSp2, we confirmed the presence of a third spidroin AcSp1 in dragline silk, a spidroin widely recognized as the major constituent of wrapping silk. Our findings also reveal that MA glands, spinning dope, and dragline silk contain at least 7 common proteins: major ampullate spidroin 1 and 2 (MaSp1 and MaSp2), 3 members of the Cysteine-Rich Protein Family (CRP1, CRP2 and CRP4), and two uncharacterized proteins, CRISP3 and fasciclin. In summary, this study provides a proteomic blueprint to construct synthetic silk fibers that most closely mimic natural fibers



To access this thesis/dissertation you must have a valid email address and log-in to Scholarly Commons.

Find in PacificSearch



If you are the author and would like to grant permission to make your work openly accessible, please email


Rights Statement

Rights Statement

In Copyright. URI:
This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).