LKEA10107 Peptide chemistry and protein modification

Responsible DepartmentDepartment of Basic Science and Environment

Earliest Possible YearMSc. 1 year to MSc. 2 year
DurationOne block
Credits7.5 (ECTS)
Level of CourseMSc
ExaminationFinal Examination

oral examination

Some Aid allowed

Description of Examination: At the oral exam, the student is given a question from a central topic in the course. Then the student has 15 min to prepare answers to this question. During this period, all aids except internet access are allowed. The student will then be questioned in this topic followed by a brief discussion of other areas of the syllabus.

Weight: 100 %

7-point scale, internal examiner
Organisation of TeachingThe course will consits of lectures (approx. 40%), classes (theoretical exercises) (approx. 27%), practical (laboratory) exercises (approx. 33%). A 'journal club' will be integrated into the lectures in the second part of the course.
Block PlacementBlock 1
Week Structure: C
Language of InstructionEnglish
Optional PrerequisitesA thorough understanding of organic chemistry (minimum requirement is an introductory and a dedicated course in organic chemistry), bioorganic chemistry, biochemistry of peptides and proteins
Mandatory PrerequisitesCompulsory for MSc students in Medicinal Chemistry. Open for Danish and international guest students.
Course Content
Solid-phase synthesis of peptides, including protecting groups, coupling reagents, linkers, resins etc., conformational aspects of biological activity of peptides and peptide derivatives, introduction to peptidomimetics, peptidomics. Examples of peptides, peptide derivatives and peptidomimetics as drugs, spectroscopic characterization of peptides, with a focus on CD spectroscopy and MS. Sequencing of peptides (Edman and MS). Methods for chemoselective chemical protein modifications relevant for biopharmaceuticals, semi-synthetic methods for obtaining modified proteins. Chemistry of post-translational modifications of proteins, including phosphorylation, glycosylation and acylation.
Teaching and learning Methods
The course will consits of lectures, classes (theoretical exercises), practical (laboratory) exercises. The lectures will be overview lectures which presents the course topics. The classes (theoretical exercises) will cover applications of the main topics and will rely active student participation. A 'journal club' will be integrated in the second part of the course. The laboratory part of the course will focus on experiemntal solid-phase peptide synthesis and on chemical modifcations of proteins using chemoselective reactions. Lecturers will be from LIFE and FARMA.
Learning Outcome
This course in peptide chemistry and basic protein modification provides comprehensive knowledge and understanding of peptides and proteins as drug candidates. The course provides the tools required for the planning of chemical synthesis of peptides and peptide derivatives, and gives an introduction to chemical modifications of proteins relevant for biopharmaceuticals. The latter include selective modification of reactive amino acid side chains and semi-synthesis of proteins. It thus provides chemical insights into the fundamentals of design of biopharmaceutical drugs, which is an area of growing interest to the pharmaceutical industry, as well as academic environments worldwide.

Enable design of solid-phase synthesis of a peptide (incl. selection of resins, linkers, protecting groups, and coupling reagents). Planning of simple chemical modifications of proteins and estimate the effect on their properties. Laboratory experiments will provide practical skills of appropriate handling of special chemicals as well as apparatus for solid-phase peptide synthesis. Both theoretical and practical understanding of methods for solid-phase synthesis of peptides and modifications of proteins will be acquired.

Application of methods for solid-phase synthesis of peptides. Description of conformational aspects relating to biological activity of peptides. Understanding of principles of peptide and peptide derivatives as drugs, including peptidomimetics. Understanding of chemical modification of proteins, including semi-synthesis of proteins and improvement of proteins as drugs. Use of basic knowledge of analytical methods such as circular dichroism (CD) spectroscopy and mass spectrometry (MS) of peptides and proteins.
Course Literature
Textbook and articles. This information will be available June 2011.
Course Coordinator
Knud Jørgen Jensen,, Department of Basic Sciences and Environment, Phone: 353-32430
Study Board
Study Committee NSN
Work Load
theoretical exercises48