Structure, Cellular Synthesis and Assembly of Biopolymers

306 Pages·1992·10.3 MB·English

by  Mehmet Sarikaya (auth.), Professor Dr. Steven T. Case (eds.)

Results and Problems in
Cell Differentiation
ASeries ofTopical Volumes in Developmental Biology
19
Editors
W. Hennig, L. Nover, and U. Scheer
Steven T. Case (Ed.)
Structure, Cellular Synthesis
and Assembly ofBiopolymers
With 128 Figures and 13 Tables
Springer-Verlag Berlin Heide1berg GmbH
Professor Dr. STEVEN T. CASE
Dept. of Biochemistry
The University ofMississippi
Medical Center
2500 North State Street
Jackson, MS 39216-4505, USA
ISBN 978-3-662-22440-3 ISBN 978-3-540-47207-0 (eBook)
DOI 10.1007/978-3-540-47207-0
Library ofCongress Cataloging-in-Publication Data
Structure, cellular synthesis, and assembly of biopolymers / Steven T. Case (ed.).
p. cm. --(Results and problems in cell differentiation; 19)
Includes bibliographical references and index.
l. Biopolymers. 2. Developmental biology.l. Case, Steven T., 1949- . H. Series.
QH607.R4 vol.19 [QP80l.B69] 574.87'612 s--dc20 [574.19'24]92-36490 CIP
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© Springer-Verlag Berlin Heidelberg 1992
Originally published by Springer-Verlag Berlin Heidelberg New York in 1992.
Softcover reprint of the hardcover 1s t edition 1992
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This book is dedicated with gratitude and affection to
PrQfessor bvin M. Gottlieb
in honor of his 70th birthday and retirement as
Professor qj'Chemistry. Widener University, Chester, PA, USA
Preface
Modern technology has enabled scientists to genera te data at an unprecedented
rate. This deluge of information can lead to two problems. With the exception of a
few dedicated colleagues, the scientific community at large is unable to compile an
overall picture of progress because of the volume and complexity of knowledge
gained. Concurrently, the investigator may lose agIobaI perspective that relates his
or her research to other apparently unrelated fields. During the past decade, I have
fallen victim to both problems.
Two valued colleagues, Drs. Donald B. Sittman and Susan A. Gerbi, for quite
different reasons, have maintained a strong interest in my research. On several
occasions, they suggested that it was time to review and consolidate data obtained
in the study of Balbiani ring genes and their encoded secretory proteins. While this
task in itself was not problematic, the context in which to pi ace this review was not
dear.
Over a span of three and a half years, I was fortunate to participate in aseries
of stimulating meetings that enabled me to interact with a dissimilar group of
scientists sharing a common interest; biopolymers. First, there were the Office of
Naval Research/Molecular Biology Program meetings for contractors in the
Bioengineering for Materials Application (lune 1987) and Biopolymers (October
1989) pro grams. Next, there was the U niversity /Industry Workshop on Biomolecu
lar Materials sponsored by the National Science Foundation (October 1990).
Finally, there was a symposium, "Materials Synthesis Based on Biological Pro
cesses," at the annual meeting of the Materials Research Society (November 1990).
Among these groups of scientists was a subset that studied a variety of naturally
occurring biomolecular materials with compositions and properties as diverse as
the organisms that fabricated them. In each instance the synthesis, assembly and
processing of these biopolymers were accomplished by a tissue composed of highly
differentiated cells. Thus, with the encouragement of Dr. Wolfgang Hennig, this
emerged as the theme of a volume in the se ries, Results and Problems in Cell
Differentiation.
The subject of this volume is an unlikely combination of biopolymers. These
natural biomaterials have unique structures and physical or mechanical properties
which may be applicable to the design of novel biomolecular materials. The intent
of this volume is to sampie, in depth, several dasses of biopolymers (nanolaminated
ceramies, adhesive proteins, eggshell pro teins and protein fibers) that are syn
thesized by a variety of organisms (mollusks, parasitic trematodes, fish and insects)
and studied by an equally diverse group of scientists (materials scientists, zoolo-
VIII Preface
gists, biochemists, molecular biologists, biophysicists and mechanical engineers).
The reader will be introduced to the biological systems in order to understand
Nature's use of each biopolymer. In each instance, highly differentiated cells are
responsible for the synthesis of biopolymer precursors. A vailable data will be
summarized according to their structure, assembly and processing. The reader will
also sam pie some of the microscopic and micromechanical methods used to
measure properties of biopolymers. Since the study of each biopolymer has an
historically unique origin and approach, our comprehension of their structures and
mechanisms of assembly is disparate. Our greatest opportunity to decipher and
exploit Nature's skills in biopolymer engineering is through the combined expertise
of interdisciplinary teams of scientists such as the contributors to this volume.
I am extremely grateful to the authors for their enthusiasm and cooperation in
the preparation and timely submission of manuscripts. They made my task
surprisingly pleasant. I wish to express my special thanks to Mrs. Alice Matthews
for expert secretarial assistance in compiling the index for this volume.
Last, but certainly not least, I wish to acknowledge the loving support of my
wife, Gay Lynn, son, Chad Erik, and daughter, Jill Lynn. Many hours that
belonged to them were sacrificed in my persuit of this endeavor.
Jackson, Mississippi, August 1992 Steven T. Case
Contents
1 Nacre of Abalone Shell:
a Natural Multifunctional Nanolaminated Ceramic-Polymer
Composite Material (With 12 Figures)
MEHMET SARIKAYA and ILHAN A. AKSAY
Introduction: Nanocomposite Materials and Biological Composites
2 Mechanical Properties of Nacre ...................................... . 3
2.1 Toughness and Strength in Nacre ..................................... . 3
2.2 Toughening Mechanisms ............................................ . 5
2.3 Strengthening Mechanisms .......................................... . 8
3 Design Guide1ines for the Processing of Biomimetic Laminated Composites 9
4 Structure of the Red Abalone Shell: Prismatic and Nacreous Layers ...... . 11
4.1 Structure of the Shell at the Macro Level .............................. . 11
4.2 Structure of the Nacre at the Nanometer Level ......................... . 12
4.2.1 Morphology of Inorganic Phase: Aragonite ............................ . 12
4.2.2 Crystallography of Aragonite Platelets ................................ . 13
5 Structure of the Organic Matrix and its Relationship to the Inorganic Phase . 20
6 Summary and Future Directions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 22
References ................................................................ 24
2 The Formation of MusseI Byssus: Anatomy
of a Natural Manufacturing Process (With 8 Figures )
J. HERBERT WAlTE
Introduction ........................................................ 27
1.1 Variations of Nature-Envy . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 27
1.2 MusseIs: Bearded Models for Industry ................................. 27
1.3 When and Why Musseis Sprouted Beards .............................. 29
1.4 Byssus is Tough Stuff . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 29
2 The Production Site in M. edulis ...................................... 31
2.1 Mussei Anatomy .................................................... 31
2.2 MusseI Foot ........................................................ 32
3 Building Blocks. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 34
3.1 Byssal Collagen. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 34
x
Contents
3.2 DOPA-Containing Proteins ............................. . . . . . . . . . . . . . . 35
3.3 Cateeholoxidase. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37
4 The Proeess for Making Byssus ....................................... 38
4.1 Cues and Preferenees ................................................ 38
4.2 Thread Formation ................................................... 40
4.3 Plaque Formation ................................................... 41
4.4 Stern Formation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 44
5 Manufaeturing Models . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 44
5.1 Themes of lndustrial Materials Proeessing ............................. 44
5.2 Extrusion and Calendering of Threads ................................. 45
5.3 SizingoftheByssus ................................................. 47
5.4 Injeetion Molding of Plaques ......................................... 48
6 Future Challenges .............................................. . . . . . 50
Referenees ................................................................ 51
3 Reflections on the Structure
of Mussel Adhesive Proteins (With 6 Figures )
RICHARD A. LAuRsEN
Adhesion in Nature ................................................. . 55
2 MusseI Adhesion ................................................... . 55
3 The Strueture of MusseI Adhesive Proteins ............................ . 56
3.1 Primary Strueture .................................................. . 56
3.1.1 Peptide Sequenee Studies ........................................... . 56
3.1.2 DNA Sequenee Studies ............................................. . 57
3.1.3 Motifs ............................................................ . 60
3.1.4 Mieroheterogeneity ................................................. . 61
3.1.5 Similarities with Other Proteins ...................................... . 62
3.1.6 Cross-Links ....................................................... . 62
3.2 Seeondary Structure ................................................ . 64
3.2.1 Do the Adhesive Proteins Have Secondary Structure? .................. . 64
3.2.2 Physicoehemical Studies ............................................ . 65
3.2.3 Antibody Cross-Reaetivity .......................................... . 65
3.2.4 Models ........................................................... . 66
3.2.4.1 Fibrous Struetural Proteins ........................................... 66
3.2.4.2 Ice Nuc1eation Protein ............................................... 67
3.2.4.3 Eggshell Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 67
3.2.4.4 MusseI Adhesive Protein: a Hypothetical Model ........................ 68
4 Assembly of Monomeric Proteins to Form a Functional Adhesive ......... 69
4.1 General Considerations .............................................. 69
4.2 Characteristics of Adhesives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
4.2.1 Adhesion and Cohesion .............................................. 69
4.2.2 Collagen-Based Glues ............................................... 70
4.3 Attainment of a Condensed State . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 70
Contents XI
4.3.1 Charge Reduetion ................................................... 70
4.3.2 Aggregation. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 71
5 Proeessing of Adhesive Proteins by the Mussei ......................... 71
6 ConcIusions ........................................................ 72
Referenees ................................................................ 72
4 Composition and Design of Fasciola hepatica Eggshells
(With 3 Figures)
ALLISON C. RICE-FICHT
Introduetion ........................................................ 75
l.1 Life CycIe of Fasciola hepatica . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
1.2 The Role of Shell Polymers and ScIerotization in Development ........... 76
2 Eggshell Morphogenesis ............................................. 76
3 Bioehemieal Charaeteristies of F hepatica Eggshell (Chorion) Proteins and
Preeursors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 80
3.1 Chemie al Stability of the Eggshell Is Based on Quinone Tanning . . . . . . . . . . 80
3.2 Protein Complement of the Eggshell; Implieations of Post-Translational
Modifieation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 81
3.3 Mieroheterogeneity of Shell Preeursors ................................ 86
3.4 Shell Assembly ..................................................... 86
4 Comparative Strategies in Eggshell Produetion ......................... 88
4.1 Gene Strueture . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 88
4.2 Expression of Chorion Proteins ...................................... . 91
Referenees ............................................................... . 92
5 The Cell and Molecular Biology of Eggshell Formation in
Schistosoma mansoni (With 6 Figures)
KIM E. WELLS and lOHN S. CORDINGLEY
1 Introduetion. An Overview of Eggshell Formation in Sehistosomes . . . . . . . . 97
2 A Survey 01' Reeent New Data ........................................ 98
2.1 Female-Speeifie Genes and Proteins Are Not Yolk Proteins .............. 98
2.2 Glyeine-Rieh and Tyrosine-Rieh Eggshell Proteins ...................... 99
2.3 The TRP Repeat Adopts a Left-Handed a-Helix in Aqueous Solution ..... 100
2.4 Eggshell Preeursors Are DOPA Proteins ............................... 101
2.5 Eggshell Preeursors Are an Aeid-Stabilized Emulsion ................... 101
2.6 Histidine Residues in TRP May Be Responsible for Stabilizing the Emulsion 102
2.7 Raising the VesicIe pH Destroys the Emulsion. . . . . . . . . . . . . . . . . . . . . . . . .. 103
3 The Meehanism of Eggshell Formation and the Role of Mehlis' Gland .... , 103
3.1 Eggshell Formation in F hepatica ..................................... 103
3.2 Extending the Pieture ................................................ 103
3.3 Triggering the Cross-Linking ......................................... 104