Max Bergmann was a German-American biochemist whose foundational work on the chemical nature of proteins and peptides changed the course of biochemistry. The methods he developed allowed scientists to investigate the structure and function of these molecules with greater precision. Bergmann’s career spanned a turbulent period of history, and his move to the United States marked a significant chapter where he continued to influence the field profoundly.
Early Life and Scientific Formation
Max Bergmann was born in Fürth, Germany, on February 12, 1886, into a Jewish family. His father was a prosperous coal merchant, and Max was the seventh of nine children. Initially, his academic interests were in botany, and he began studying biology at the University of Munich. He soon became captivated by organic chemistry after attending lectures by the influential chemist Adolf von Baeyer, which prompted him to change his field of study.
Bergmann’s scientific path was shaped at the University of Berlin under Nobel laureate Emil Fischer, a leading figure in the study of natural products. After earning his Ph.D. in 1911, Bergmann became Fischer’s research assistant until Fischer’s death in 1919. This period involved research on amino acids, carbohydrates, and tannins, laying the groundwork for his future investigations into protein chemistry.
In 1921, Bergmann was appointed the first director of the Kaiser Wilhelm Institute for Leather Research in Dresden. The institute required him to balance scientific inquiry with practical applications. He established one of the world’s leading laboratories for protein chemistry, which set the stage for his most significant contributions.
Pioneering Research in Protein Chemistry
At his Dresden laboratory, Bergmann focused on protein structure and the specificity of enzymes. He and his colleagues developed new analytical methods to break down proteins and identify their constituent amino acids. This work provided strong evidence that a protein’s properties are dictated by the specific arrangement of these amino acids.
A significant area of his research involved proteolytic enzymes, which break down proteins. Bergmann’s work on enzymes like papain demonstrated that they operate with high chemical specificity, recognizing and cleaving specific peptide bonds. To study this, his lab had to create small peptide chains as substrates, which highlighted the limitations of existing synthetic techniques.
These investigations led Bergmann and his colleague Carl Niemann to propose that amino acids in proteins were arranged in a recurring pattern. While this hypothesis was later proven to be an oversimplification, it stimulated significant experimental work. The challenge of synthesizing peptides to test such theories underscored the need for a more reliable method, a problem his laboratory would soon solve.
The Carbobenzoxy Method Breakthrough
The need for a reliable way to synthesize peptides of a defined sequence led to a major achievement. In 1932, Bergmann and his collaborator Leonidas Zervas developed the carbobenzoxy method for peptide synthesis. This technique provided a controlled way to link amino acids in a specific order, a previously difficult task.
The method uses a “protecting group,” the carbobenzoxy chloride group (Cbz or Z-group), which is attached to the nitrogen atom (amino group) of an amino acid. Protecting this end of the molecule prevents unwanted side reactions. This ensures the other end (the carboxyl group) can be activated to form a peptide bond with the next amino acid in the sequence.
After the peptide bond is formed, the protecting group is removed through hydrogenolysis, a process that does not damage the new chain. This cycle of protection, coupling, and deprotection can be repeated to build longer peptides one amino acid at a time. The Bergmann-Zervas synthesis was the first widely applicable method for creating peptides with a known structure, enabling detailed studies of hormones, antibiotics, and enzymes.
Later Career and Lasting Influence
The rise of the Nazi regime in Germany forced Bergmann, who was of Jewish descent, to leave his home and position in 1933. He emigrated to the United States and in 1934 joined the Rockefeller Institute for Medical Research in New York. There, he re-established his laboratory, and his research program continued to focus on protein structure and enzyme action, influencing American molecular biology.
At Rockefeller, Bergmann mentored a new generation of scientists, including Stanford Moore and William H. Stein. Moore and Stein began their work under his guidance and later continued his research on protein analysis. Their development of highly sensitive chromatographic techniques earned them the Nobel Prize in Chemistry in 1972.
Max Bergmann died in New York City on November 7, 1944, at the age of 58. The methods he pioneered and the intellectual tradition he fostered in his laboratories in both Germany and the United States had a lasting impact on biochemistry and molecular biology.