Common eland, Taurotragus oryx
Credit: David Clode / Unsplash.
Some 60,000 years ago, humans occupying a shelter in southern Africa left behind traces of activities that modern science is only now learning to recover. An ochre-rich surface at Kilpdrift Shelter preserves proteins identified as belonging to the common eland, Taurotragus oryx, a large African antelope.
For those who insist that the entire Universe was created only a few thousand years ago, the difficulty begins before we even consider what these people were doing: they were already there, handling animal materials and ochre, tens of thousands of years before the supposed creation of their ancestors.
The discovery is described in a paper published in Proceedings of the Royal Society B by researchers from Kyushu University, the University of Bergen and the University of Copenhagen.
What that contribution represents remains an open question. Animal-derived material may have been deliberately mixed with ochre, or the surface may preserve traces of eland hides treated with it. The finding establishes an association between ochre and animal material; it does not, by itself, establish a particular recipe, a hide-processing technique or a symbolic purpose. Nevertheless, it opens a valuable window onto the technical, and possibly symbolic, behaviour of early Homo sapiens, particularly in environments where ancient DNA is poorly preserved.
Here, then, is another example of archaeology producing inconvenient evidence for biblical literalism simply by investigating the human past. The researchers are asking what people did, which materials they used and how surviving molecules can help reconstruct their activities. There is room for uncertainty about the precise activity recorded on this ancient surface. That uncertainty is not permission to compress 60,000 years of human history into a creationist chronology of six to ten thousand years.
Ancient proteins^ recovering the invisible archaeological record. Archaeology is no longer restricted to objects and remains visible to the naked eye. Even where a hide or other animal material has disappeared, surviving molecules may preserve evidence of its former presence. Palaeoproteomics — the study of ancient proteins — allows researchers to investigate some of these otherwise invisible traces.
How can a protein identify an animal?
Proteins consist of chains of amino acids. Their sequences are inherited, and differences between species can help identify the organisms from which they came. Collagen, an abundant structural protein in tissues including skin, tendons and bone, is particularly useful in archaeological investigations.
Researchers extract protein material and analyse shorter chains called peptides. Liquid chromatography separates components of the mixture, while tandem mass spectrometry measures peptide ions and their fragmentation patterns. Comparisons with reference sequences can then identify proteins and, where sufficiently diagnostic sequences survive, narrow down their biological source. Not every peptide identifies a species: many sequences are shared by related animals.
In the Klipdrift investigation, the researchers identified type-I collagen attributed to common eland in sediment from an approximately 60,000-year-old ochre-rich surface. This reveals an association between animal material and ochre that would be difficult to establish from the surface's appearance alone.
Shouldn't collagen have decayed long ago?
Most of the original protein may indeed have decayed. Detecting identifiable traces does not mean that an intact hide, fresh tissue or a complete, functioning protein has survived. Loss of a tissue's recognisable structure and disappearance of every informative molecular fragment are different things.
Nor do proteins have a universal expiry date. Their survival depends on temperature, moisture, acidity, microbial activity and the surrounding material. Conditions that expose proteins to water and microbial enzymes can accelerate destruction; other conditions can slow it. Association with minerals can help protect some protein sequences. A decay rate measured in one environment therefore cannot simply be applied to every archaeological deposit.
This distinction has practical consequences. A study of archaeological bones detected collagen peptides even in a specimen with a reported collagen yield of 0% under conventional assessment. “No recoverable bulk collagen” and “no detectable collagen sequences” are not equivalent statements.
There is also direct evidence for much longer preservation under particular conditions. Research on ostrich eggshell recovered protein sequences from material approximately 3.8 million years old and demonstrated the protective importance of binding to the shell's mineral surface. These were eggshell proteins, not collagen, so their survival does not supply a decay rate for the Klipdrift material. It does refute the blanket assertion that identifiable protein sequences cannot survive beyond a few thousand years.
None of this establishes precisely what protected the Klipdrift collagen. In particular, finding it alongside ochre does not, by itself, prove that ochre caused its preservation. That is a separate question requiring evidence.
How do researchers distinguish ancient traces from contamination?
Contamination is a real concern, which is why ancient-protein research requires careful laboratory procedures and authentication. Relevant checks include laboratory blanks, the reliability of sequence identifications, archaeological context and patterns of molecular damage. No single damage marker is an infallible clock: chemical alteration also depends on environmental conditions and sample treatment.
The scientific response to an unexpected surviving molecule is therefore to test its identity, authenticity and preservation history. Merely declaring that “proteins decay” neither demonstrates contamination nor overturns the dating of its archaeological context. To infer a recent origin, one would need evidence that actually supports a recent origin.
What does the eland collagen tell us?
The finding supports an association between eland-derived material and an ochre-rich surface. Deliberate mixing of animal material with ochre and the presence of ochre-treated hides are possible explanations. Identifying the protein does not yet distinguish between them, or establish that the activity was symbolic.
That combination — recovering previously inaccessible evidence while acknowledging what it cannot yet resolve — is precisely how science advances.
Researchers Found Eland Collagen on a 60,000-Year-Old Ochre Surface
Traces of eland collagen may reveal how animal materials were associated with ochre during the Stone Age.
As explained in the Kyushu University report reproduced in TechnologyNetworks, the team analysed archived sediment samples using palaeoproteomics — the study of ancient proteins. Mass spectrometry and comparisons with reference databases identified type-I collagen from eland, revealing an animal contribution to an archaeological surface whose organic traces might otherwise have remained undetected.
Cpmmon eland, Taurotragus oryxCredit: David Clode / Unsplash.
: Publishing in the journal Proceedings of the Royal Society B: Biological Sciences a research team from Kyushu University, Universitetet i Bergen, and the University of Copenhagen reports that they found traces of ancient collagen protein from the common eland, Taurotragus oryx, on a 60,000-year-old ochre-rich surface in the Kilpdrift Complex, a Middle and Later Stone Age archaeological site located within the coastal cliffs of the De Hoop Nature Reserve in South Africa.
To better understand how ochre was used by early humans, the team used palaeoproteomics, the high-throughput analyses of ancient proteins, to search for potential proteinaceous traces within this archaeological feature. The study identified collagen from elands in the ochre surface, suggesting that either animal-derived materials were deliberately mixed with the ochre or ochre-treated eland hides were present at the site.
These findings provide new evidence for the complex technical and possibly symbolic behaviors of early Homo sapiens.
Eland collagen links ochre to animal materials
The most significant finding is the identification of type I collagen proteins from the common eland, which provides biomolecular evidence that animal-derived materials were associated with ochre use during the Middle Stone Age. Until now, evidence of organic components mixed with ochre has been extremely rare, especially in Africa.
This discovery offers a new way to investigate how early humans used ochre and other organic materials in their daily, technical, and potentially symbolic activities.
An eland is a large plains antelope found in East and Southern Africa.
First author Zahra Haghighi pictured preparing a sample in a clean laboratory for paleoproteomic analysis.
Credit: Takumi Tsutaya/Kyushu University
Tracing proteins through sediment
The team analyzed archived sediment samples taken from the Klipdrif Complex using palaeoproteomics, a growing field of archaeology and paleontology that examines ancient proteins preserved in materials collected at archaeological sites. The proteins were extracted from the sediments and analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS).
The resulting protein fragments were then compared to large protein databases and a custom collagen reference database to identify their species of origin.
These findings demonstrate that palaeoproteomics can successfully recover and identify ancient proteins from archaeological sediments, even in challenging African environments where ancient DNA rarely survives.
This creates a powerful new tool for archaeologists studying early human behavior, allowing them to investigate biological materials no longer visible in the archaeological record.
Publication:
Once again, an investigation into the human past has produced evidence that sits comfortably within the scientific understanding of our history but far outside the cramped chronology of biblical literalism. Around 60,000 years ago, people at Klipdrift were leaving traces of activities involving ochre and animal materials. Whatever the precise purpose of those activities, these people lived tens of thousands of years before young-Earth creationism permits humans — or even Earth itself — to have existed.
The surviving collagen offers no escape from that chronological difficulty. Identifying ancient protein traces is not the same as finding fresh tissue, and the fact that proteins decay does not establish that every identifiable fragment must disappear within a few thousand years. A claim of recent origin requires evidence, not an assumed expiry date for organic molecules. The relevant questions concern preservation conditions, molecular identification, contamination and archaeological context — all matters for investigation rather than theological assertion.
There are uncertainties here, and the researchers acknowledge them. The association between eland collagen and ochre does not yet tell us whether people were preparing a mixture, treating hides or undertaking an activity with symbolic significance. That distinction between what the evidence establishes and what remains open is a strength of science. Uncertainty about what people were doing is not evidence that they lived at some entirely different time.
The researchers did not need to set out to refute Genesis. They simply asked questions about an ancient surface and recovered another small piece of human history. As so often happens, the difficulty for creationism lies in the answers that nature supplies.
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